Emeritus Professor Mitchell Guss

Professor

G08 - Biochemistry and Microbiology Building
The University of Sydney

Telephone +61 2 9351 4302
Fax +61 2 9351 4726

Research interests

Mitchell Guss has a long standing interest in the application of the tools of structural biology to understand how biological molecules work and how they can be exploited for medical and other purposes.

Selected grants

2012

  • Molecular foundations for essential fine tuning of regulatory signals in healthy heart function; Trewhella J, Guss M; Australian Research Council (ARC)/Discovery Projects (DP).

2011

  • POLARStar Omega; Sunde M, Guss M, Mackay J, Matthews J, Payne R, Cubeddu L; National Health and Medical Research Council (NHMRC)/Equipment Grants.
  • LMO2-containing complexes in leukemia and blood cell development; Matthews J, Mackay J, Guss M; National Health and Medical Research Council (NHMRC)/Project Grants.

2010

  • Federated Single Crystal X-ray Structural Analysis Facility; Kepert C, Guss M, Malby R, Jormakka M, Cole M, Dixon N, Kearley G; Australian Research Council (ARC)/Linkage Infrastructure, Equipment and Facilities (LIEF).

2009

  • Molecular Mechanisms of two-component signal transduction in bacteria; Trewhella J, Guss M; Australian Research Council (ARC)/Discovery Projects (DP).

2008

  • Bacterial monooxygenases as new biocatalysts; Holmes A, Coleman N, Guss M; Australian Research Council (ARC)/Discovery Projects (DP).
  • Transcriptional complexes in haematopiesis and T-cell Leukaemia; Matthews J, Guss M, Trewhella J; National Health and Medical Research Council (NHMRC)/Project Grants.
  • Inhibition of histidine kinase signal sensing: a novel paradigm for antimicrobial development; King G, Guss M, Trewhella J; National Health and Medical Research Council (NHMRC)/Project Grants.

2006

  • Structure-based inhibitor design of VAP-1/SSAO for the treatment of respiratory dirsorders and other major inflammatory diseases; Guss M, McDonald I, Collyer C, McDonald I; Australian Research Council (ARC)/Linkage Projects (LP).
  • e-Research Infrastructure for the Molecular and Materials Structure Sciences; Turner P, Martin J, Guss M, Kepert C; Australian Research Council (ARC)/Linkage Infrastructure, Equipment and Facilities (LIEF).
  • The structure and function of dihydroorotase - an enzyme essential for pyrimidine biosynthesis; Guss M; Australian Research Council (ARC)/Discovery Projects (DP).

2005

  • Metalloproteins and metalloenzymes; Dooley D, Guss M, Freeman H; Australian Research Council (ARC)/Discovery Projects (DP).
  • Structural characterisation of a natural inhibitor of sporulation bound to its histidine kinase target; Guss M; National Health and Medical Research Council (NHMRC)/Project Grants.

2004

  • The molecular basis for the control of sporulation in Bacillus subtilis; Guss M; DVC Research/Research and Development Scheme: Research and Development (R&D).

2003

  • The structural basis for the action of anticancer DNA-intercalating topoisomerase poisons; Adams A, Guss M; National Health and Medical Research Council (NHMRC)/Project Grants.

2002

  • High performance protein crystallography; Curmi J, Mabbutt B, Ollis D, Dixon N, Guss M; Australian Research Council (ARC)/Linkage Infrastructure, Equipment and Facilities (LIEF).
  • Understanding and changing the mechanism of an enzyme: converting a peptidase to a phosphotriesterase; Guss M, Freeman H; Australian Research Council (ARC)/Discovery Projects (DP).
  • Structural studies of catalysis and electron transfer by copper proteins; Freeman H, Guss M; Australian Research Council (ARC)/Discovery Projects (DP).
  • Generic Account Code for travel under the Access to Major Research Facilities Program _ Dr M Guss; Guss M; Australian Nuclear Science and Technology Organisation/Major Research Facilities Program.

2001

  • ANSTO travel grant-Australian Synchrotron Research Program; Guss M; Australian Nuclear Science and Technology Organisation/Australian Synchrotron Research Program.
  • Enhancement of hydrolytic activity of organophosporus degrading enzymes; Guss M; DVC Research/Bridging Support Grant.
  • Structural characterisation of complexes between peptide toxins and their receptors; Guss M; DVC Research/Research and Development Scheme: Research and Development (R&D).

2000

  • Structures and mechanisms of metalloproteins; Guss M, Freeman H; Australian Research Council (ARC)/Large Research Grants (LRG).
  • DynaPro-MS/X laser light scattering equipment; Guss M; National Health and Medical Research Council (NHMRC)/Equipment Grants.
  • The 3-dimensional structure of anticancer drug-DNA complexes determined by crystallography; Guss M, Denny W; National Health and Medical Research Council (NHMRC)/Project Grants.

Selected publications

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Book Chapters

  • Jacques, D., Guss, M., Trewhella, J. (2012). Antikinases: Their Structures and Roles in Two-component Signalling. In Roy Gross, Dagmar Beier (Eds.), Two-component Systems in Bacteria, (pp. 163-180). Norfolk, United Kingdom: Caister Academic Press.

Journals

  • Michie, K., Kwan, A., Tung, C., Guss, M., Trewhella, J. (2016). A Highly Conserved Yet Flexible Linker Is Part of a Polymorphic Protein-Binding Domain in Myosin-Binding Protein C. Structure, 24(11), 2000-2007. [More Information]
  • Nadvi, N., Michie, K., Kwan, A., Guss, M., Trewhella, J. (2016). Clinically Linked Mutations in the Central Domains of Cardiac Myosin-Binding Protein C with Distinct Phenotypes Show Differential Structural Effects. Structure, 24(1), 105-115. [More Information]
  • Fung, H., Gadd, M., Drury, T., Cheung, S., Guss, M., Coleman, N., Matthews, J. (2015). Biochemical and biophysical characterisation of haloalkane dehalogenases DmrA and DmrB in Mycobacterium strain JS60 and their role in growth on haloalkanes. Molecular Microbiology, 97(3), 439-453. [More Information]
  • Wilkinson-White, L., Lester, K., Ripin, N., Jacques, D., Guss, M., Matthews, J. (2015). GATA1 directly mediates interactions with closely spaced pseudopalindromic but not distantly spaced double GATA sites on DNA. Protein Science, 24(10), 1649-1659. [More Information]
  • McGrath, A., Laming, E., Casas Garcia, G., Kvansakul, M., Guss, M., Trewhella, J., Calmes, B., Bernhardt, P., Hanson, G., Kappler, U., et al (2015). Structural basis of interprotein electron transfer in bacterial sulfite oxidation. eLife, 4, 1-26. [More Information]
  • Dickson, C., Jacques, D., Clubb, R., Guss, M., Gell, D. (2015). The structure of haemoglobin bound to the haemoglobin receptor IsdH from Staphylococcus aureus shows disruption of the native [alpha]-globin haem pocket. Acta Crystallographica. Section D: Biological Crystallography, 71(Pt 6), 1295-1306. [More Information]
  • Guss, M., McMahon, B. (2014). How to make deposition of images a reality. Acta Crystallographica. Section D: Biological Crystallography, 70(Pt 10), 2520-2532. [More Information]
  • Dickson, C., Krishna Kumar, K., Jacques, D., Malmirchegini, G., Spirig, T., Mackay, J., Clubb, R., Guss, M., Gell, D. (2014). Structure of the Hemoglobin-IsdH Complex Reveals the Molecular Basis of Iron Capture by Staphylococcus aureus. The Journal of Biological Chemistry, 289(10), 6728-6738. [More Information]
  • Kumar, K., Jacques, D., Guss, M., Gell, D. (2014). The structure of a-haemoglobin in complex with a haemoglobin-binding domain from Staphylococcus aureus reveals the elusive a-haemoglobin dimerization interface. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, F70(8), 1032-1037. [More Information]
  • Gadd, M., Jacques, D., Nisevic, I., Craig, V., Kwan, A., Guss, M., Matthews, J. (2013). A Structural Basis for the Regulation of the LIM Homeodomain Protein Islet 1 (Isl1) by Intra- and Intermolecular Interactions. Journal of Biological Chemistry, 288(30), 21924-21935. [More Information]
  • Vandevenne, M., Jacques, D., Artuz, C., Nguyen, C., Kwan, A., Segal, D., Matthews, J., Crossley, M., Guss, M., Mackay, J. (2013). New insights into DNA recognition by zinc fingers revealed by structural analysis of the oncoprotein ZNF217. Journal of Biological Chemistry, 288(15), 10616-10627. [More Information]
  • Gadd, M., Jacques, D., Guss, M., Matthews, J. (2012). Crystallization and diffraction of an Isl1-Ldb1 complex. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 68(11), 1398-1401. [More Information]
  • Guss, M. (2012). Hans Charles Freeman (1929–2008): A scientific journey from dipole moments to protein crystallography. Journal of Inorganic Biochemistry, 115, 114-118. [More Information]
  • Jacques, D., Guss, M., Svergun, D., Trewhella, J. (2012). Publication guidelines for structural modelling of small-angle scattering data from biomolecules in solution. Acta Crystallographica. Section D: Biological Crystallography, D68(6), 620-626. [More Information]
  • Jacques, D., Guss, M., Trewhella, J. (2012). Reliable structural interpretation of small-angle scattering data from bio-molecules in solution - the importance of quality control and a standard reporting framework. B M C Structural Biology, 12, 1-3. [More Information]
  • Ash, M., Maher, M., Guss, M., Jormakka, M. (2012). The cation-dependent G-proteins: In a class of their own. FEBS Letters, 586(16), 2218-2224. [More Information]
  • Lu, Y., Kwan, A., Jeffries, C., Guss, M., Trewhella, J. (2012). The Motif of Human Cardiac Myosin-binding Protein C Is Required for Its Ca2+ -dependent Interaction with Calmodulin. Journal of Biological Chemistry, 287(37), 31596-31607. [More Information]
  • Laming, E., McGrath, A., Guss, M., Kappler, U., Maher, M. (2012). The X-ray crystal structure of a pseudoazurin from Sinorhizobium meliloti. Journal of Inorganic Biochemistry, 115, 148-154. [More Information]
  • Jacques, D., Langley, D., Hynson, R., Whitten, A., Kwan, A., Guss, M., Trewhella, J. (2011). A Novel Structure of an Antikinase and Its Inhibitor. Journal of Molecular Biology, 405(1), 214-226. [More Information]
  • Ash, M., Maher, M., Guss, M., Jormakka, M. (2011). A suite of Switch I and Switch II mutant structures from the G-protein domain of FeoB. Acta Crystallographica. Section D: Biological Crystallography, 67(11), 973-980. [More Information]
  • Ernberg, K., Zhong, B., Ko, K., Miller, L., Nguyen, Y., Sayre, L., Guss, M., Lee, I. (2011). Structural and enzyme activity studies demonstrate that aryl substituted 2,3-butadienamine analogs inactivate Arthrobacter globiformis amine oxidase (AGAO) by chemical derivatization of the 2,4,5-trihydroxyphenylalanine quinone (TPQ) cofactor. Biochimica et Biophysica Acta. Proteins and Proteomics, 1814 (5), 638-646. [More Information]
  • Krishna Kumar, K., Jacques, D., Pishchany, G., Caradoc-Davies, T., Spirig, T., Malmirchegini, G., Langley, D., Dickson, C., Mackay, J., Clubb, R., Guss, M., et al (2011). Structural Basis for Hemoglobin Capture by Staphylococcus aureus Cell-surface Protein, IsdH. Journal of Biological Chemistry, 286(44), 38439-38447. [More Information]
  • Gadd, M., Bhati, M., Jeffries, C., Langley, D., Trewhella, J., Guss, M., Matthews, J. (2011). Structural Basis for Partial Redundancy in a Class of Transcription Factors, the LIM Homeodomain Proteins, in Neural Cell Type Specification. Journal of Biological Chemistry, 286(50), 42971-42980. [More Information]
  • McGrath, A., Mithieux, S., Collyer, C., Bakhuis, J., van den Berg, M., Sein, A., Heinz, A., Schmelzer, C., Weiss, A., Guss, M. (2011). Structure and Activity of Aspergillus nidulans Copper Amine Oxidase. Biochemistry, 50(25), 5718-5730. [More Information]
  • Ash, M., Maher, M., Guss, M., Jormakka, M. (2011). The initiation of GTP hydrolysis by the g-domain of FeoB: Insights from a transition-state complex structure. PloS One, 6(8), 1-10. [More Information]
  • Ash, M., Maher, M., Guss, M., Jormakka, M. (2011). The structure of an N11A mutant of the G-protein domain of FeoB. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 67(12), 1511-1515. [More Information]
  • Jacques, D., Langley, D., Kuramitsu, S., Yokoyama, S., Trewhella, J., Guss, M. (2011). The structure of TTHA0988 from Thermus thermophilus, a KipI-KipA homologue incorrectly annotated as an allophanate hydrolase. Acta Crystallographica. Section D: Biological Crystallography, 67(2), 105-111. [More Information]
  • McGrath, A., Hilmer, K., Collyer, C., Dooley, D., Guss, M. (2010). A new crystal form of human diamine oxidase. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 66(2), 137-142. [More Information]
  • Ernberg, K., McGrath, A., Peat, T., Adams, T., Xiao, X., Pham, T., Newman, J., McDonald, I., Collyer, C., Guss, M. (2010). A new crystal form of human vascular adhesion protein 1. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 66(Pt 12), 1572-1578. [More Information]
  • Chow, J., Jeffries, C., Kwan, A., Guss, M., Trewhella, J. (2010). Calmodulin Disrupts the Structure of the HIV-1 MA Protein. Journal of Molecular Biology, 400(4), 702-714. [More Information]
  • McGrath, A., Caradoc-Davies, T., Collyer, C., Guss, M. (2010). Correlation of Active Site Metal Content in Human Diamine Oxidase with Trihydroxyphenylalanine Quinone Cofactor Biogenesis. Biochemistry, 49(38), 8316-8324. [More Information]
  • Ash, M., Guilfoyle, A., Clarke, R., Guss, M., Maher, M., Jormakka, M. (2010). Potassium-activated GTPase reaction in the G protein-coupled ferrous iron transporter B. Journal of Biological Chemistry, 285(19), 14594-14602. [More Information]
  • Langley, D., Shojaei, M., Chan, C., Lok, H., Mackay, J., Traut, T., Guss, M., Christopherson, R. (2009). Corrections. Biochemistry, 48(11), 2569-2570. [More Information]
  • Gadd, M., Langley, D., Guss, M., Matthews, J. (2009). Crystallization and diffraction of an Lhx4-Isl2 complex. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, F65(2), 151-153. [More Information]
  • Guss, M. (2009). Hans C. Freeman (1929-2008). Acta Crystallographica. Section D: Biological Crystallography, 65(1), 93-95. [More Information]
  • McGrath, A., Hilmer, K., Collyer, C., Shephard, E., Elmore, B., Brown, D., Dooley, D., Guss, M. (2009). Structure and inhibition of human diamine oxidase. Biochemistry, 48(41), 9810-9822. [More Information]
  • Jacques, D., Streamer, M., Rowland, S., King, G., Guss, M., Trewhella, J., Langley, D. (2009). Structure of the sporulation histidine kinase inhibitor Sda from Bacillus subtilis and insights into its solution state. Acta Crystallographica. Section D: Biological Crystallography, 65(6), 574-581. [More Information]
  • Lee, M., del Rosario, M., Harris, H., Blankenship, R., Guss, M., Freeman, H. (2009). The crystal structure of auracyanin A at 1.85 A resolution: The structures and functions of auracyanins A and B, two almost identical "blue" copper proteins, in the photosynthetic bacterium Chloroflexus aurantiacus. Journal of Biological Inorganic Chemistry, 14(3), 329-345. [More Information]
  • Loughlin, F., Mansfield, R., Vaz, P., McGrath, A., Setiyaputra, S., Gamsjaeger, R., Chen, E., Morris, B., Guss, M., Mackay, J. (2009). The zinc fingers of the SR-like protein ZRANB2 are single-stranded RNA-binding domains that recognize 5' splice site-like sequences. Proceedings of the National Academy of Sciences of the United States of America (PNAS), 106(14), 5581-5586. [More Information]
  • Graham, S., Guss, M. (2008). Complexes of mutants of Escherichia coli aminopeptidase P and the tripeptide substrate ValProLeu. Archives of Biochemistry and Biophysics, 469(2), 200-208. [More Information]
  • Langley, D., Trambaiolo, D., Duff, A., Dooley, D., Freeman, H., Guss, M. (2008). Complexes of the copper-containing amine oxidase from Arthrobacter globiformis with the inhibitors benzylhydrazine and tranylcypromine. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, F64(7), 577-583. [More Information]
  • Loughlin, F., Lee, M., Guss, M., Mackay, J. (2008). Crystallization of a ZRANB2-RNA complex. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 64(Pt 12), 1175-1177. [More Information]
  • Bhati, M., Lee, M., Nancarrow, A., Bach, I., Guss, M., Matthews, J. (2008). Crystallization of an Lhx3-Isl1 complex. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 64(4), 297-299. [More Information]
  • Langley, D., Brown, D., Cheruzel, L., Contakes, S., Duff, A., Hilmer, K., Dooley, D., Gray, H., Guss, M., Freeman, H. (2008). Enantiomer-specific binding of ruthenium(II) molecular wires by the amine oxidase of Arthrobacter globiformis. Journal of the American Chemical Society, 130(25), 8069-8078. [More Information]
  • Jacques, D., Langley, D., Jeffries, C., Cunningham, K., Burkholder, W., Guss, M., Trewhella, J. (2008). Histidine Kinase Regulation by a Cyclophilin-like Inhibitor. Journal of Molecular Biology, 384(2), 422-435. [More Information]
  • Bhati, M., Lee, C., Nancarrow, A., Lee, M., Craig, V., Bach, I., Guss, M., Mackay, J., Matthews, J. (2008). Implementing the LIM code: the structural basis for cell type-specific assembly of LIM-homeodomain complexes. The EMBO Journal, 27, 2018-2029. [More Information]
  • Langley, D., Shojaei, M., Chan, C., Lok, H., Mackay, J., Traut, T., Guss, M., Christopherson, R. (2008). Structure and Inhibition of Orotidine 5'-Monophosphate Decarboxylase from Plasmodium falciparum. Biochemistry, 47(12), 3842-3854. [More Information]
  • Langley, D., Harty, D., Jacques, N., Hunter, N., Guss, M., Collyer, C. (2008). Structure of N-acetyl-B-D-glucosaminidase (GcnA) from the Endocarditis Pathogen Streptococcus gordonii and its Complex with the Mechanism-based Inhibitor NAG-thiazoline. Journal of Molecular Biology, 377, 104-116. [More Information]
  • Lee, M., Maher, M., Christopherson, R., Guss, M. (2007). Kinetic and Structural Analysis of Mutant Escherichia coli Dihydroorotases: A Flexible Loop Stabilizes the Transition State(,). Biochemistry, 46(37), 10538-10550. [More Information]
  • Lee, M., Maher, M., Guss, M. (2007). Structure of the T109S mutant of Escherichia coli dihydroorotase complexed with the inhibiter 5-fluoroorotate: catalytic activity is reflected by the crystal form. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 63(Part 3), 154-161. [More Information]
  • Lee, M., Chan, C., Graham, S., Christopherson, R., Guss, M., Maher, M. (2007). Structures of ligand-free and inhibitor complexes of dihydroorotase from Escherichia coli: Implications for loop movement in inhibitor design. Journal of Molecular Biology, 370(5), 812-825. [More Information]
  • Whitten, A., Jacques, D., Hammouda, B., Hanley, T., King, G., Guss, M., Trewhella, J., Langley, D. (2007). The Structure of the KinA-Sda complex suggests an allosteric mechanism of histidine kinase inhibition. Journal of Molecular Biology, 368(2), 407-420. [More Information]
  • Duff, A., Shepard, E., Langley, D., Dooley, D., Freeman, H., Guss, M. (2006). A C-terminal disulfide bond in the copper-containing amine oxidase from pea seedlings violates the twofold symmetry of the molecular dimer. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, F62(12), 1168-1173. [More Information]
  • Graham, S., Lilley, P., Lee, M., Schaeffer, P., Kralicek, A., Dixon, N., Guss, M. (2006). Kinetic and crystallographic analysis of mutant Escherichia coli aminopeptidase P: insights into substrate recognition and the mechanism of catalysis. Biochemistry, 45(3), 964-975. [More Information]
  • Jeffries, C., Graham, S., Stokes, P., Collyer, C., Guss, M., Matthews, J. (2006). Stabilization of a binary protein complex by intein-mediated cyclization. Protein Science, 15(11), 2612-2618. [More Information]
  • Duff, A., Cohen, A., Ellis, P., Hilmer, K., Langley, D., Dooley, D., Freeman, H., Guss, M. (2006). The 1.23 A structure of Pichia pastoris lysyl oxidase reveals a lysine-lysine cross-link. Acta Crystallographica. Section D: Biological Crystallography, 62(9), 1073-1084. [More Information]
  • Langley, D., Duff, A., Freeman, H., Guss, M. (2006). The copper-containing amine oxidase from Arthrobacter globiformis: refinement at 1.55 and 2.20 A resolution in two crystal forms. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 62(11), 1052-1057. [More Information]
  • Sträter, N., Jasper, B., Scholte, M., Krebs, B., Duff, A., Langley, D., Han, R., Averill, B., Freeman, H., Guss, M. (2005). Crystal structures of recombinant human purple Acid phosphatase with and without an inhibitory conformation of the repression loop. Journal of Molecular Biology, 351(1), 233-246. [More Information]
  • Lee, M., Chan, C., Guss, M., Christopherson, R., Maher, M. (2005). Dihydroorotase from Escherichia coli: loop movement and cooperativity between subunits. Journal of Molecular Biology, 348(3), 523-533. [More Information]
  • Contakes, S., Juda, G., Langley, D., Halpern-Manners, N., Duff, A., Dunn, A., Gray, H., Dooley, D., Guss, M., Freeman, H. (2005). Reversible inhibition of copper amine oxidase activity by channel-blocking ruthenium(II) and rhenium(I) molecular wires. Proceedings of the National Academy of Sciences of the United States of America (PNAS), 102(38), 13451-13456. [More Information]
  • Graham, S., Bond, C., Freeman, H., Guss, M. (2005). Structural and Functional Implications of Metal Ion Selection in Aminopeptidase P, a Metalloprotease with a Dinuclear Metal Center. Biochemistry, 44(42), 13820-13836. [More Information]
  • Adams, A., Leong, C., Denny, W., Guss, M. (2005). Structures of two minor-groove-binding quinolinium quaternary salts complexed with d(CGCGAATTCGCG)(2) at 1.6 and 1.8 Angstrom resolution. Acta Crystallographica. Section D: Biological Crystallography, 61(10), 1348-1353. [More Information]
  • Langley, D., Harty, D., Graham, S., Guss, M., Hunter, N., Collyer, C. (2004). Crystallization Of Gcna, An N-Acetyl-β-D-Glucosaminidase, From Streptococcus Gordonii. Acta Crystallographica. Section D: Biological Crystallography, D60, 1910-1911.
  • O'Connell, K., Langley, D., Shepard, E., Duff, A., Jeon, H., Sun, G., Freeman, H., Guss, M., Sayre, L., Dooley, D. (2004). Differential Inhibition Of Six Copper Amine Oxidases By A Family Of 4-(Aryloxy)-2-Butynamines: Evidence For A New Mode Of Inactivation. Biochemistry, 43(34), 10965-10978.
  • Maher, M., Cross, M., Wilce, M., Guss, M., Wedd, A. (2004). Metal-Substituted Derivatives Of The Rubredoxin From Clostridium Pasteurianum. Acta Crystallographica. Section D: Biological Crystallography, 60(2), 298-303.
  • Adams, A., Guss, M., Denny, W., Wakelin, L. (2004). Structure Of 9-Amino- N-(2-Dimethylamino)Propyl Acridine-4-Carboxamide Bound To D(Cgtacg)(2): A Comparison Of Structures Of D(Cgtacg)(2) Complexed With Intercalators In The Presence Of Cobalt. Acta Crystallographica. Section D: Biological Crystallography, 60(5), 823-828.
  • Graham, S., Maher, M., Simmons, W., Freeman, H., Guss, M. (2004). Structure Of Escherichia Coli Aminopeptidase P In Complex With The Inhibitor Apstatin. Acta Crystallographica. Section D: Biological Crystallography, 60(10), 1770-1779.
  • Maher, M., Ghosh, M., Grunden, A., Menon, A., Adams, M., Freeman, H., Guss, M. (2004). Structure Of The Prolidase From Pyrococcus Furiosus. Biochemistry, 43(10), 2771-2783.
  • Deane, J., Ryan, D., Sunde, M., Maher, M., Guss, M., Visvader, J., Matthews, J. (2004). Tandem Lim Domains Provide Synergistic Binding In The LMO4:Ldb1 Complex. The EMBO Journal, 23(18), 3589-3598.
  • Duff, A., Trambaiolo, D., Cohen, A., Ellis, P., Juda, G., Shepard, E., Langley, D., Dooley, D., Freeman, H., Guss, M. (2004). Using Xenon As A Probe For Dioxygen-Binding Sites In Copper Amine Oxidases. Journal of Molecular Biology, 344(3), 599-607.
  • Graham, S., Lee, M., Freeman, H., Guss, M. (2003). An orthorhombic form of Escherichia coli aminopeptidase P at 2.4 A resolution. Acta Crystallographica. Section D: Biological Crystallography, 59(5), 897-902.
  • Lee, M., Maher, M., Freeman, H., Guss, M. (2003). Auracyanin B structure in space group P65. Acta Crystallographica. Section D: Biological Crystallography, 59(9), 1545-1550.
  • Deane, J., Maher, M., Langley, D., Graham, S., Visvader, J., Guss, M., Matthews, J. (2003). Crystallization of FLINC4, an intramolecular LM04-ldb1 complex. Acta Crystallographica. Section D: Biological Crystallography, 59(8), 1484-1486.
  • Maher, M., Huang, D., Guss, M., Collyer, C., Christopherson, R. (2003). Crystallization of hamster dihydroorotase: involvement of a disulfide-linked tetrameric form. Acta Crystallographica. Section D: Biological Crystallography, 59(2), 381-384.
  • Duff, A., Cohen, A., Ellis, P., Kuchar, J., Langley, D., Shepard, E., Dooley, D., Freeman, H., Guss, M. (2003). The Crystal Structure of Pichia pastoris Lysyl Oxidase. Biochemistry, 42(51), 15148-15157.
  • Adams, A., Guss, M., Denny, W., Wakelin, L. (2002). Crystal structure of 9-amino-N-[2-(4-morpholinyl)ethyl]-4-acridinecarboxamide bound to d(CGTACG)2: implications for structure-activity relationships of acridinecarboxamide topoisimerase poisons. Nucleic Acids Research, 30(3), 719-725.
  • Lee, M., Willingham, K., Langley, D., Maher, M., Cohen, A., Ellis, P., Kuchar, J., Dooley, D., Freeman, H., Guss, M. (2002). Crystallization of Pichia pastoris lysyl oxidase. Acta Crystallographica. Section D: Biological Crystallography, 58(12), 2177-2179.
  • Bond, C., Guss, M., Maher, M., Wilce, J., Willingham, K., Freeman, H., Blankenship, R., Selvaraj, F. (2001). Crystal structure of Auracyanin, a "Blue" copper protein from the green thermophilic photosynthetic bacterium Chloroflexus aurantiacus. Journal of Molecular Biology, 306, 47-67.
  • Willingham, K., Maher, M., Guss, M., Freeman, H., Ghosh,, M., Adams, M., Grunden, A. (2001). Crystallization and characterization of the prolidase from Pyrococcus furiosus. Acta Crystallographica. Section D: Biological Crystallography, 57, 428-430.
  • Guss, M., Harel, M., Kasher, R., Nicolas,, A., Balass,, M., Fridkin, M., Smit, A., Brejc, K., Sixma, T., Katchalski-Katzir, E., et al (2001). The binding site of acetylcholine receptor as visualised in the x-ray structure of a complex between a-Bungarotoxin and a mimotape peptide. Neuron, 32, 265-275.

2016

  • Michie, K., Kwan, A., Tung, C., Guss, M., Trewhella, J. (2016). A Highly Conserved Yet Flexible Linker Is Part of a Polymorphic Protein-Binding Domain in Myosin-Binding Protein C. Structure, 24(11), 2000-2007. [More Information]
  • Nadvi, N., Michie, K., Kwan, A., Guss, M., Trewhella, J. (2016). Clinically Linked Mutations in the Central Domains of Cardiac Myosin-Binding Protein C with Distinct Phenotypes Show Differential Structural Effects. Structure, 24(1), 105-115. [More Information]

2015

  • Fung, H., Gadd, M., Drury, T., Cheung, S., Guss, M., Coleman, N., Matthews, J. (2015). Biochemical and biophysical characterisation of haloalkane dehalogenases DmrA and DmrB in Mycobacterium strain JS60 and their role in growth on haloalkanes. Molecular Microbiology, 97(3), 439-453. [More Information]
  • Wilkinson-White, L., Lester, K., Ripin, N., Jacques, D., Guss, M., Matthews, J. (2015). GATA1 directly mediates interactions with closely spaced pseudopalindromic but not distantly spaced double GATA sites on DNA. Protein Science, 24(10), 1649-1659. [More Information]
  • McGrath, A., Laming, E., Casas Garcia, G., Kvansakul, M., Guss, M., Trewhella, J., Calmes, B., Bernhardt, P., Hanson, G., Kappler, U., et al (2015). Structural basis of interprotein electron transfer in bacterial sulfite oxidation. eLife, 4, 1-26. [More Information]
  • Dickson, C., Jacques, D., Clubb, R., Guss, M., Gell, D. (2015). The structure of haemoglobin bound to the haemoglobin receptor IsdH from Staphylococcus aureus shows disruption of the native [alpha]-globin haem pocket. Acta Crystallographica. Section D: Biological Crystallography, 71(Pt 6), 1295-1306. [More Information]

2014

  • Guss, M., McMahon, B. (2014). How to make deposition of images a reality. Acta Crystallographica. Section D: Biological Crystallography, 70(Pt 10), 2520-2532. [More Information]
  • Dickson, C., Krishna Kumar, K., Jacques, D., Malmirchegini, G., Spirig, T., Mackay, J., Clubb, R., Guss, M., Gell, D. (2014). Structure of the Hemoglobin-IsdH Complex Reveals the Molecular Basis of Iron Capture by Staphylococcus aureus. The Journal of Biological Chemistry, 289(10), 6728-6738. [More Information]
  • Kumar, K., Jacques, D., Guss, M., Gell, D. (2014). The structure of a-haemoglobin in complex with a haemoglobin-binding domain from Staphylococcus aureus reveals the elusive a-haemoglobin dimerization interface. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, F70(8), 1032-1037. [More Information]

2013

  • Gadd, M., Jacques, D., Nisevic, I., Craig, V., Kwan, A., Guss, M., Matthews, J. (2013). A Structural Basis for the Regulation of the LIM Homeodomain Protein Islet 1 (Isl1) by Intra- and Intermolecular Interactions. Journal of Biological Chemistry, 288(30), 21924-21935. [More Information]
  • Vandevenne, M., Jacques, D., Artuz, C., Nguyen, C., Kwan, A., Segal, D., Matthews, J., Crossley, M., Guss, M., Mackay, J. (2013). New insights into DNA recognition by zinc fingers revealed by structural analysis of the oncoprotein ZNF217. Journal of Biological Chemistry, 288(15), 10616-10627. [More Information]

2012

  • Jacques, D., Guss, M., Trewhella, J. (2012). Antikinases: Their Structures and Roles in Two-component Signalling. In Roy Gross, Dagmar Beier (Eds.), Two-component Systems in Bacteria, (pp. 163-180). Norfolk, United Kingdom: Caister Academic Press.
  • Gadd, M., Jacques, D., Guss, M., Matthews, J. (2012). Crystallization and diffraction of an Isl1-Ldb1 complex. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 68(11), 1398-1401. [More Information]
  • Guss, M. (2012). Hans Charles Freeman (1929–2008): A scientific journey from dipole moments to protein crystallography. Journal of Inorganic Biochemistry, 115, 114-118. [More Information]
  • Jacques, D., Guss, M., Svergun, D., Trewhella, J. (2012). Publication guidelines for structural modelling of small-angle scattering data from biomolecules in solution. Acta Crystallographica. Section D: Biological Crystallography, D68(6), 620-626. [More Information]
  • Jacques, D., Guss, M., Trewhella, J. (2012). Reliable structural interpretation of small-angle scattering data from bio-molecules in solution - the importance of quality control and a standard reporting framework. B M C Structural Biology, 12, 1-3. [More Information]
  • Ash, M., Maher, M., Guss, M., Jormakka, M. (2012). The cation-dependent G-proteins: In a class of their own. FEBS Letters, 586(16), 2218-2224. [More Information]
  • Lu, Y., Kwan, A., Jeffries, C., Guss, M., Trewhella, J. (2012). The Motif of Human Cardiac Myosin-binding Protein C Is Required for Its Ca2+ -dependent Interaction with Calmodulin. Journal of Biological Chemistry, 287(37), 31596-31607. [More Information]
  • Laming, E., McGrath, A., Guss, M., Kappler, U., Maher, M. (2012). The X-ray crystal structure of a pseudoazurin from Sinorhizobium meliloti. Journal of Inorganic Biochemistry, 115, 148-154. [More Information]

2011

  • Jacques, D., Langley, D., Hynson, R., Whitten, A., Kwan, A., Guss, M., Trewhella, J. (2011). A Novel Structure of an Antikinase and Its Inhibitor. Journal of Molecular Biology, 405(1), 214-226. [More Information]
  • Ash, M., Maher, M., Guss, M., Jormakka, M. (2011). A suite of Switch I and Switch II mutant structures from the G-protein domain of FeoB. Acta Crystallographica. Section D: Biological Crystallography, 67(11), 973-980. [More Information]
  • Ernberg, K., Zhong, B., Ko, K., Miller, L., Nguyen, Y., Sayre, L., Guss, M., Lee, I. (2011). Structural and enzyme activity studies demonstrate that aryl substituted 2,3-butadienamine analogs inactivate Arthrobacter globiformis amine oxidase (AGAO) by chemical derivatization of the 2,4,5-trihydroxyphenylalanine quinone (TPQ) cofactor. Biochimica et Biophysica Acta. Proteins and Proteomics, 1814 (5), 638-646. [More Information]
  • Krishna Kumar, K., Jacques, D., Pishchany, G., Caradoc-Davies, T., Spirig, T., Malmirchegini, G., Langley, D., Dickson, C., Mackay, J., Clubb, R., Guss, M., et al (2011). Structural Basis for Hemoglobin Capture by Staphylococcus aureus Cell-surface Protein, IsdH. Journal of Biological Chemistry, 286(44), 38439-38447. [More Information]
  • Gadd, M., Bhati, M., Jeffries, C., Langley, D., Trewhella, J., Guss, M., Matthews, J. (2011). Structural Basis for Partial Redundancy in a Class of Transcription Factors, the LIM Homeodomain Proteins, in Neural Cell Type Specification. Journal of Biological Chemistry, 286(50), 42971-42980. [More Information]
  • McGrath, A., Mithieux, S., Collyer, C., Bakhuis, J., van den Berg, M., Sein, A., Heinz, A., Schmelzer, C., Weiss, A., Guss, M. (2011). Structure and Activity of Aspergillus nidulans Copper Amine Oxidase. Biochemistry, 50(25), 5718-5730. [More Information]
  • Ash, M., Maher, M., Guss, M., Jormakka, M. (2011). The initiation of GTP hydrolysis by the g-domain of FeoB: Insights from a transition-state complex structure. PloS One, 6(8), 1-10. [More Information]
  • Ash, M., Maher, M., Guss, M., Jormakka, M. (2011). The structure of an N11A mutant of the G-protein domain of FeoB. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 67(12), 1511-1515. [More Information]
  • Jacques, D., Langley, D., Kuramitsu, S., Yokoyama, S., Trewhella, J., Guss, M. (2011). The structure of TTHA0988 from Thermus thermophilus, a KipI-KipA homologue incorrectly annotated as an allophanate hydrolase. Acta Crystallographica. Section D: Biological Crystallography, 67(2), 105-111. [More Information]

2010

  • McGrath, A., Hilmer, K., Collyer, C., Dooley, D., Guss, M. (2010). A new crystal form of human diamine oxidase. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 66(2), 137-142. [More Information]
  • Ernberg, K., McGrath, A., Peat, T., Adams, T., Xiao, X., Pham, T., Newman, J., McDonald, I., Collyer, C., Guss, M. (2010). A new crystal form of human vascular adhesion protein 1. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 66(Pt 12), 1572-1578. [More Information]
  • Chow, J., Jeffries, C., Kwan, A., Guss, M., Trewhella, J. (2010). Calmodulin Disrupts the Structure of the HIV-1 MA Protein. Journal of Molecular Biology, 400(4), 702-714. [More Information]
  • McGrath, A., Caradoc-Davies, T., Collyer, C., Guss, M. (2010). Correlation of Active Site Metal Content in Human Diamine Oxidase with Trihydroxyphenylalanine Quinone Cofactor Biogenesis. Biochemistry, 49(38), 8316-8324. [More Information]
  • Ash, M., Guilfoyle, A., Clarke, R., Guss, M., Maher, M., Jormakka, M. (2010). Potassium-activated GTPase reaction in the G protein-coupled ferrous iron transporter B. Journal of Biological Chemistry, 285(19), 14594-14602. [More Information]

2009

  • Langley, D., Shojaei, M., Chan, C., Lok, H., Mackay, J., Traut, T., Guss, M., Christopherson, R. (2009). Corrections. Biochemistry, 48(11), 2569-2570. [More Information]
  • Gadd, M., Langley, D., Guss, M., Matthews, J. (2009). Crystallization and diffraction of an Lhx4-Isl2 complex. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, F65(2), 151-153. [More Information]
  • Guss, M. (2009). Hans C. Freeman (1929-2008). Acta Crystallographica. Section D: Biological Crystallography, 65(1), 93-95. [More Information]
  • McGrath, A., Hilmer, K., Collyer, C., Shephard, E., Elmore, B., Brown, D., Dooley, D., Guss, M. (2009). Structure and inhibition of human diamine oxidase. Biochemistry, 48(41), 9810-9822. [More Information]
  • Jacques, D., Streamer, M., Rowland, S., King, G., Guss, M., Trewhella, J., Langley, D. (2009). Structure of the sporulation histidine kinase inhibitor Sda from Bacillus subtilis and insights into its solution state. Acta Crystallographica. Section D: Biological Crystallography, 65(6), 574-581. [More Information]
  • Lee, M., del Rosario, M., Harris, H., Blankenship, R., Guss, M., Freeman, H. (2009). The crystal structure of auracyanin A at 1.85 A resolution: The structures and functions of auracyanins A and B, two almost identical "blue" copper proteins, in the photosynthetic bacterium Chloroflexus aurantiacus. Journal of Biological Inorganic Chemistry, 14(3), 329-345. [More Information]
  • Loughlin, F., Mansfield, R., Vaz, P., McGrath, A., Setiyaputra, S., Gamsjaeger, R., Chen, E., Morris, B., Guss, M., Mackay, J. (2009). The zinc fingers of the SR-like protein ZRANB2 are single-stranded RNA-binding domains that recognize 5' splice site-like sequences. Proceedings of the National Academy of Sciences of the United States of America (PNAS), 106(14), 5581-5586. [More Information]

2008

  • Graham, S., Guss, M. (2008). Complexes of mutants of Escherichia coli aminopeptidase P and the tripeptide substrate ValProLeu. Archives of Biochemistry and Biophysics, 469(2), 200-208. [More Information]
  • Langley, D., Trambaiolo, D., Duff, A., Dooley, D., Freeman, H., Guss, M. (2008). Complexes of the copper-containing amine oxidase from Arthrobacter globiformis with the inhibitors benzylhydrazine and tranylcypromine. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, F64(7), 577-583. [More Information]
  • Loughlin, F., Lee, M., Guss, M., Mackay, J. (2008). Crystallization of a ZRANB2-RNA complex. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 64(Pt 12), 1175-1177. [More Information]
  • Bhati, M., Lee, M., Nancarrow, A., Bach, I., Guss, M., Matthews, J. (2008). Crystallization of an Lhx3-Isl1 complex. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 64(4), 297-299. [More Information]
  • Langley, D., Brown, D., Cheruzel, L., Contakes, S., Duff, A., Hilmer, K., Dooley, D., Gray, H., Guss, M., Freeman, H. (2008). Enantiomer-specific binding of ruthenium(II) molecular wires by the amine oxidase of Arthrobacter globiformis. Journal of the American Chemical Society, 130(25), 8069-8078. [More Information]
  • Jacques, D., Langley, D., Jeffries, C., Cunningham, K., Burkholder, W., Guss, M., Trewhella, J. (2008). Histidine Kinase Regulation by a Cyclophilin-like Inhibitor. Journal of Molecular Biology, 384(2), 422-435. [More Information]
  • Bhati, M., Lee, C., Nancarrow, A., Lee, M., Craig, V., Bach, I., Guss, M., Mackay, J., Matthews, J. (2008). Implementing the LIM code: the structural basis for cell type-specific assembly of LIM-homeodomain complexes. The EMBO Journal, 27, 2018-2029. [More Information]
  • Langley, D., Shojaei, M., Chan, C., Lok, H., Mackay, J., Traut, T., Guss, M., Christopherson, R. (2008). Structure and Inhibition of Orotidine 5'-Monophosphate Decarboxylase from Plasmodium falciparum. Biochemistry, 47(12), 3842-3854. [More Information]
  • Langley, D., Harty, D., Jacques, N., Hunter, N., Guss, M., Collyer, C. (2008). Structure of N-acetyl-B-D-glucosaminidase (GcnA) from the Endocarditis Pathogen Streptococcus gordonii and its Complex with the Mechanism-based Inhibitor NAG-thiazoline. Journal of Molecular Biology, 377, 104-116. [More Information]

2007

  • Lee, M., Maher, M., Christopherson, R., Guss, M. (2007). Kinetic and Structural Analysis of Mutant Escherichia coli Dihydroorotases: A Flexible Loop Stabilizes the Transition State(,). Biochemistry, 46(37), 10538-10550. [More Information]
  • Lee, M., Maher, M., Guss, M. (2007). Structure of the T109S mutant of Escherichia coli dihydroorotase complexed with the inhibiter 5-fluoroorotate: catalytic activity is reflected by the crystal form. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 63(Part 3), 154-161. [More Information]
  • Lee, M., Chan, C., Graham, S., Christopherson, R., Guss, M., Maher, M. (2007). Structures of ligand-free and inhibitor complexes of dihydroorotase from Escherichia coli: Implications for loop movement in inhibitor design. Journal of Molecular Biology, 370(5), 812-825. [More Information]
  • Whitten, A., Jacques, D., Hammouda, B., Hanley, T., King, G., Guss, M., Trewhella, J., Langley, D. (2007). The Structure of the KinA-Sda complex suggests an allosteric mechanism of histidine kinase inhibition. Journal of Molecular Biology, 368(2), 407-420. [More Information]

2006

  • Duff, A., Shepard, E., Langley, D., Dooley, D., Freeman, H., Guss, M. (2006). A C-terminal disulfide bond in the copper-containing amine oxidase from pea seedlings violates the twofold symmetry of the molecular dimer. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, F62(12), 1168-1173. [More Information]
  • Graham, S., Lilley, P., Lee, M., Schaeffer, P., Kralicek, A., Dixon, N., Guss, M. (2006). Kinetic and crystallographic analysis of mutant Escherichia coli aminopeptidase P: insights into substrate recognition and the mechanism of catalysis. Biochemistry, 45(3), 964-975. [More Information]
  • Jeffries, C., Graham, S., Stokes, P., Collyer, C., Guss, M., Matthews, J. (2006). Stabilization of a binary protein complex by intein-mediated cyclization. Protein Science, 15(11), 2612-2618. [More Information]
  • Duff, A., Cohen, A., Ellis, P., Hilmer, K., Langley, D., Dooley, D., Freeman, H., Guss, M. (2006). The 1.23 A structure of Pichia pastoris lysyl oxidase reveals a lysine-lysine cross-link. Acta Crystallographica. Section D: Biological Crystallography, 62(9), 1073-1084. [More Information]
  • Langley, D., Duff, A., Freeman, H., Guss, M. (2006). The copper-containing amine oxidase from Arthrobacter globiformis: refinement at 1.55 and 2.20 A resolution in two crystal forms. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 62(11), 1052-1057. [More Information]

2005

  • Sträter, N., Jasper, B., Scholte, M., Krebs, B., Duff, A., Langley, D., Han, R., Averill, B., Freeman, H., Guss, M. (2005). Crystal structures of recombinant human purple Acid phosphatase with and without an inhibitory conformation of the repression loop. Journal of Molecular Biology, 351(1), 233-246. [More Information]
  • Lee, M., Chan, C., Guss, M., Christopherson, R., Maher, M. (2005). Dihydroorotase from Escherichia coli: loop movement and cooperativity between subunits. Journal of Molecular Biology, 348(3), 523-533. [More Information]
  • Contakes, S., Juda, G., Langley, D., Halpern-Manners, N., Duff, A., Dunn, A., Gray, H., Dooley, D., Guss, M., Freeman, H. (2005). Reversible inhibition of copper amine oxidase activity by channel-blocking ruthenium(II) and rhenium(I) molecular wires. Proceedings of the National Academy of Sciences of the United States of America (PNAS), 102(38), 13451-13456. [More Information]
  • Graham, S., Bond, C., Freeman, H., Guss, M. (2005). Structural and Functional Implications of Metal Ion Selection in Aminopeptidase P, a Metalloprotease with a Dinuclear Metal Center. Biochemistry, 44(42), 13820-13836. [More Information]
  • Adams, A., Leong, C., Denny, W., Guss, M. (2005). Structures of two minor-groove-binding quinolinium quaternary salts complexed with d(CGCGAATTCGCG)(2) at 1.6 and 1.8 Angstrom resolution. Acta Crystallographica. Section D: Biological Crystallography, 61(10), 1348-1353. [More Information]

2004

  • Langley, D., Harty, D., Graham, S., Guss, M., Hunter, N., Collyer, C. (2004). Crystallization Of Gcna, An N-Acetyl-β-D-Glucosaminidase, From Streptococcus Gordonii. Acta Crystallographica. Section D: Biological Crystallography, D60, 1910-1911.
  • O'Connell, K., Langley, D., Shepard, E., Duff, A., Jeon, H., Sun, G., Freeman, H., Guss, M., Sayre, L., Dooley, D. (2004). Differential Inhibition Of Six Copper Amine Oxidases By A Family Of 4-(Aryloxy)-2-Butynamines: Evidence For A New Mode Of Inactivation. Biochemistry, 43(34), 10965-10978.
  • Maher, M., Cross, M., Wilce, M., Guss, M., Wedd, A. (2004). Metal-Substituted Derivatives Of The Rubredoxin From Clostridium Pasteurianum. Acta Crystallographica. Section D: Biological Crystallography, 60(2), 298-303.
  • Adams, A., Guss, M., Denny, W., Wakelin, L. (2004). Structure Of 9-Amino- N-(2-Dimethylamino)Propyl Acridine-4-Carboxamide Bound To D(Cgtacg)(2): A Comparison Of Structures Of D(Cgtacg)(2) Complexed With Intercalators In The Presence Of Cobalt. Acta Crystallographica. Section D: Biological Crystallography, 60(5), 823-828.
  • Graham, S., Maher, M., Simmons, W., Freeman, H., Guss, M. (2004). Structure Of Escherichia Coli Aminopeptidase P In Complex With The Inhibitor Apstatin. Acta Crystallographica. Section D: Biological Crystallography, 60(10), 1770-1779.
  • Maher, M., Ghosh, M., Grunden, A., Menon, A., Adams, M., Freeman, H., Guss, M. (2004). Structure Of The Prolidase From Pyrococcus Furiosus. Biochemistry, 43(10), 2771-2783.
  • Deane, J., Ryan, D., Sunde, M., Maher, M., Guss, M., Visvader, J., Matthews, J. (2004). Tandem Lim Domains Provide Synergistic Binding In The LMO4:Ldb1 Complex. The EMBO Journal, 23(18), 3589-3598.
  • Duff, A., Trambaiolo, D., Cohen, A., Ellis, P., Juda, G., Shepard, E., Langley, D., Dooley, D., Freeman, H., Guss, M. (2004). Using Xenon As A Probe For Dioxygen-Binding Sites In Copper Amine Oxidases. Journal of Molecular Biology, 344(3), 599-607.

2003

  • Graham, S., Lee, M., Freeman, H., Guss, M. (2003). An orthorhombic form of Escherichia coli aminopeptidase P at 2.4 A resolution. Acta Crystallographica. Section D: Biological Crystallography, 59(5), 897-902.
  • Lee, M., Maher, M., Freeman, H., Guss, M. (2003). Auracyanin B structure in space group P65. Acta Crystallographica. Section D: Biological Crystallography, 59(9), 1545-1550.
  • Deane, J., Maher, M., Langley, D., Graham, S., Visvader, J., Guss, M., Matthews, J. (2003). Crystallization of FLINC4, an intramolecular LM04-ldb1 complex. Acta Crystallographica. Section D: Biological Crystallography, 59(8), 1484-1486.
  • Maher, M., Huang, D., Guss, M., Collyer, C., Christopherson, R. (2003). Crystallization of hamster dihydroorotase: involvement of a disulfide-linked tetrameric form. Acta Crystallographica. Section D: Biological Crystallography, 59(2), 381-384.
  • Duff, A., Cohen, A., Ellis, P., Kuchar, J., Langley, D., Shepard, E., Dooley, D., Freeman, H., Guss, M. (2003). The Crystal Structure of Pichia pastoris Lysyl Oxidase. Biochemistry, 42(51), 15148-15157.

2002

  • Adams, A., Guss, M., Denny, W., Wakelin, L. (2002). Crystal structure of 9-amino-N-[2-(4-morpholinyl)ethyl]-4-acridinecarboxamide bound to d(CGTACG)2: implications for structure-activity relationships of acridinecarboxamide topoisimerase poisons. Nucleic Acids Research, 30(3), 719-725.
  • Lee, M., Willingham, K., Langley, D., Maher, M., Cohen, A., Ellis, P., Kuchar, J., Dooley, D., Freeman, H., Guss, M. (2002). Crystallization of Pichia pastoris lysyl oxidase. Acta Crystallographica. Section D: Biological Crystallography, 58(12), 2177-2179.

2001

  • Bond, C., Guss, M., Maher, M., Wilce, J., Willingham, K., Freeman, H., Blankenship, R., Selvaraj, F. (2001). Crystal structure of Auracyanin, a "Blue" copper protein from the green thermophilic photosynthetic bacterium Chloroflexus aurantiacus. Journal of Molecular Biology, 306, 47-67.
  • Willingham, K., Maher, M., Guss, M., Freeman, H., Ghosh,, M., Adams, M., Grunden, A. (2001). Crystallization and characterization of the prolidase from Pyrococcus furiosus. Acta Crystallographica. Section D: Biological Crystallography, 57, 428-430.
  • Guss, M., Harel, M., Kasher, R., Nicolas,, A., Balass,, M., Fridkin, M., Smit, A., Brejc, K., Sixma, T., Katchalski-Katzir, E., et al (2001). The binding site of acetylcholine receptor as visualised in the x-ray structure of a complex between a-Bungarotoxin and a mimotape peptide. Neuron, 32, 265-275.

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