Peter Moody

Personal Details

Peter Moody	Professor of Structural Biology
	Department: Molecular and Cell Biology Telephone: +44 (0)116 229 7097 Email: peter.moody@le.ac.uk Address: Lancaster Rd, LE1 7HB Web Links: https://www2.le.ac.uk/departments/molcellbiol https://www2.le.ac.uk/institutes/liscb

Biography

I am Professor of Structural Biology. I read Biochemistry at York, with a final year project using X-ray crystallography to determine the structure of a small bacterial ribonuclease. I continued using X-ray crystallography for my PhD in the Physics Department at Imperial College, London with studies of the mechanism of the glycolytic enzyme Glyceraldehyde 3-Phosphate Dehydrogenase. After my PhD I continued to use protein crystallography to investigate enzyme mechanisms at Harvard, Imperial College and at York. I took a post at Leicester in 1995, where I work on the structures and mechanisms of redox and other enzymes, using X-ray crystallography to determine structures and neutron crystallography in order see the positions of hydrogen atoms.

A list of my Protein Data Bank depositions can be found here: PDB entries

ResearcherID: A-6832-2008 ORCHID ID: 0000-0003-1762-9238

Qualifications

BA (Biochemistry) University of York, 1980
Ph.D. (Biophysics), DIC, Imperial College, University of London, 1984

Teaching

Most of my undergraduate and post-graduate teaching reflects my research interests: the structure of proteins, how enzymes work, and the methods of structural biology, particularly protein crystallography.

Publications

Freeman, S.L., Kwon H., Portolano N., Parkin G., Venkatraman Girija U., Basran J.,Fielding A.J., Fairall L., Svistunenko D.A., Moody P.C.E., Schwabe J.W.R., . Kyriacou C.P., & Raven E.L (2019) Heme binding to human CLOCK affects interactions with the E-box. Proc. Natl. Acad Sci. (USA) https://doi.org/10.1073/pnas.1905216116
Forsyth, V.T., & Moody, P.C.E. (2018) Neutron scattering for the study of biological systems – major opportunities within a rapidly changing landscape. Acta Cryst. D74, 1126-1128 https://doi.org/10.1107/S2059798318017886
Ashkar, R.; Bilheux, H.; Bordallo, H. ; Briber, R.; Callaway, D.; Cheng, X.; Chu, X.-Q.; Curtis, J.; Dadmun, M.; Fenimore, P. Fushman, D.; Gabel,F. Gupta, K.; Herberle, F.; Heinrich, F.; Hong, L.; Katsaras, J. ; Kelman, Z.; Kharlampieva, E.; Kneller, G.R.; Kovalevskyi, A.; Krueger, S.; Langan, P.; Libermann, R.;Liu, Y.; Losche, M.; Lyman, E.; Mao, Y. Marino, J.; Mattos, C.; Meilleur, F.; Moody, P.; Nickels, J.D.; O’Dell, W.; O’Neill, H.; Perez-Salas, U.; Peters, J.; Petridis, L.; Sokolov, A.; Stanley, C.; Wagner, N.; Weinrich, M.; Weiss, K. Wymore, T.; Zhang, Y.; Smith, J.C. (2018). Neutron scattering in the biological sciences: progress and prospects. Acta Cryst. D74, 1129-1168 https://doi.org/10.1107/S2059798318017503
H Kwon, PS Langan, L Coates, EL Raven & PCE Moody (2018) "The rise of neutron cryo-crystallography" Acta Cryst. D74, 792-799 https://doi.org/10.1107/S205979831800640X
SM Kapetenaki, MJ Burton, J Basran, C Uragami, PCE Moody, JS Mitcheson, R Schmid, NW Davies, P Dorlet, M Vos, NM Storey, & EL Raven (2018) "A mechanism for CO regulation of ion channels" Nature Communications
JOM Almitairi, U Venkatraman Girija, CM Furze, X Simpson-Gray, F Badakshi, JE Marshall, WJ Schwaeble, DA Mitchell, PCE Moody & R Wallis (2018) Structure of the C1r–C1s interaction of the C1 complex of complement activation. Proc. Natl. Acad. Sci. (USA)
PCE Moody & EL Raven (2018) The Nature & Reactivity of Ferryl Heme in Compounds I and II Acc. Chem Res.
DD Turner, L Lad, H Kwon, J Basran, KH Carr, PCE Moody & EL Raven (2017) The role of Ala134 in controlling substrate binding and reactivity in ascorbate peroxidase J. Inorg. Biochem.
H Kwon, J Basran, CM Casadei, AJ Fielding, TE Schrader, A Ostermann, JM Devos, P Aller, MP Blakeley, PCE Moody & EL Raven (2016) Direct visualization of a Fe(IV)–OH intermediate in a heme enzyme Nature Communications 7, Article number: 13445 (2016) This paper was selected for F1000Prime, as being of exceptional significance in its field: F1000 Prime link
H Kwon, O Smith, EL Raven & PCE Moody (2017) Combining X-ray and Neutron Crystallography with Spectroscopy. Acta Cryst D72 141- 147
MJ Burton, SM Kapetanaki, T Chernova, AG Jamieson, P Dorlet, J Santolini, PCE Moody, JS Mitcheson, NW Davies, R Schmid, EL Raven, & NM Storey (2016) Heme-binding domain controls regulation of ATP-dependent potassium channels. Proc. Natl. Acad. Sci. (USA).113(14) 3785-3790
CI Nnamchi, G Parkin, I Efimov, J Basran, H Kwon, DA Svistunenko, J Agirre, BN Okolo, A Moneke, BC Nwanguma, PCE Moody & EL Raven (2016) Structural and spectroscopic characterisation of a heme peroxidase from sorghum. Journal of Biological Inorganic Chemistry 21, 63-70
H Kwon, PCE Moody & EL Raven (2016). Understanding the Reactivity and Intermediates of Peroxidases with Substrates. In Heme Peroxidases (Ed. E Raven & B. Dunford) Royal Society of Chemistry
JE Marshall, BHA Faraj, AR Gingras, R Lonnen, A Sheikh, M El-Mezgueldi, PCE Moody, & R Wallis (2015). The Crystal Structure of Pneumolysin at 2.0 Å Resolution Reveals the Molecular Packing of the Pre-pore Complex. Scientific Reports 5 Article number: 13293 (2015)
UV Girija,CM Furze,AR Gingras,T Yoshizaki,K Ohtani, JE Marshall, AK Wallis, WJ Schwaeble, M El-Mezgueldi, DA Mitchell, PCE Moody, N Wakamiya, R Wallis (2015). Molecular basis of sugar recognition by collectin-K1 and the effects of mutations associated with 3MC syndrome. BMC Biology
CM Casadei, A Gumiero, CL Metcalfe, EJ Murphy, J Basran, MG Concilio, SCM Teixeira,TE Schrader, AJ Fielding, A Ostermann, MP Blakeley, EL Raven & PCE Moody (2014) Neutron cryo-crystallography captures the protonation state of ferryl heme in a peroxidase. Science345; 193-197 This paper was selected for F1000Prime, as being of exceptional significance in its field: F1000Prime link.
M Rhyan Puno, NA Patel, SG Møller, CV Robinson, PCE Moody & M Odell (2013) Structure of Cu(I)-Bound DJ-1 Reveals a Biscysteinate Metal Binding Site at the Homodimer Interface: Insights into Mutational Inactivation of DJ-1 in Parkinsonism J. Am. Chem. Soc. 135; 15974-15977
W-C Huang, J Ellis, PCE Moody, EL Raven & GCK Roberts (2013). Redox-linked domain movements in the catalytic cycle of cytochrome P450 reductase, Structure 21(9) 1581-1589
UV Girja, AR Gingras, J Marshall, R Panchal, A Sheikh, J Harper, P Gal, WJ Schwaeble, DA Mitchell, PCE Moody & R Wallis (2013) Structural basis of the C1q/C1s interaction and its central role in assembly of the C1 complex of complement activation Proc. Natl. Acad. Sci. (USA). 110(34); 13916-13920
A Guimero, SK Badyal, T Leeks, PCE Moody & EL Raven (2013) Probing the conformational mobility of the active site of a heme peroxidase Dalton Transactions 42; 3170 – 3175
N Chauhan, J Basran, BSA Rafice, I Efimov, BS Millett, CG Mowat, PCE Moody, S Handa & EL Raven (2012) How is the distal pocket of a heme protein optimised for binding of tryptophan? FEBS Journal 279;4501-4509
EJ Murphy, CL Metcalfe, C Nnamchi, PCE Moody & EL Raven (2012) Crystal structures of guaiacol and phenol bound to a heme peroxidase FEBS Journal 279; 1632-1639
AR Gingras, UV Girija, AH Keeble, R Panchal, DA Mitchell, PCE Moody and R Wallis (2011) Structural basis of mannan-binding lectin recognition by its associated serine protease MASP-1: implications for complement activation Structure 19; 1635-1643
I Efimov SK Badyal CL Metcalfe, IK Macdonald A Gumiero EL Raven & PCE Moody (2011) Proton delivery to ferryl heme in a heme peroxidase: Enzymatic use of the Grotthuss Mechanism J. Am. Chem. Soc. 133; 15376-15383
A Gumiero, CL Metcalfe, AR Pearson, EL Raven & PCE Moody (2011). The nature of the ferryl heme in compounds I and II. J. Biol. Chem. 286; 1260-1268
DS Tourigny, PR Elliott, LJ Edgell, GM Hudson and PCE Moody (2011) Expression, purification, crystallization and preliminary X-ray analysis of the wild type and an active site mutant of glyceraldehyde-3-phosphate dehydrogenase from Campylobacter jejuni. Acta Cryst. F67; 72-75
J Purves, A Cockayne, PCE Moody & JA Morrissey (2010) Comparison of the regulation, metabolic function and role in virulence of the Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) homologues gapA and gapB in Staphylococcus aureus. Infection & Immunity 78; 5223 - 5232.
A Gumiero, EJ Murphy, CL Metcalfe, PCE Moody & EL Raven, (2010) An analysis of substrate binding interactions in the heme peroxidase enzymes: a structural perspective. Arch. Biochem. Biophys. 500; 13-20
SK Badyal, G Eaton, S Mistry, Z Pipirou, J Basran, CL Metcalfe, A Gumiero, S Handa, PCE Moody & EL Raven (2009) Evidence for Heme Oxygenase Activity in a Heme Peroxidase. Biochemistry 48; 4738–4746
EJ Murphy, CL Metcalfe, J Basran, PCE Moody & EL Raven (2008) Engineering the Substrate Specificity and Reactivity of a Heme Protein. Biochemistry 47; 13933-13941
PR Elliott, D Evans, J Greenwood and PCE Moody (2008) Expression, purification, crystallisation and preliminary X-ray analysis of a NADP-dependent Glyceraldehyde-3-phosphate Dehydrogenase from Helicobacter pylori. Acta Cryst F 64; 723-726
PR Elliott, S Mohammad, H.J Melrose and PCE Moody (2008) Expression, purification, crystallisation and preliminary X-ray analysis of a NAD-dependent Glyceraldehyde-3-phosphate dehydrogenase from Helicobacter pylori. Acta Cryst F 64; 727-729
N Chauhan, J Basran, I Efimov, D Svistunenko, HE Seward, PCE Moody and EL Raven (2008) The role of serine 167 in human indoleamine 2,3-dioxygenase: a comparison with tryptophan 2,3-dioxygenase. Biochemistry 47;4671-4789
SK Badyal, CL Metcalfe, J Basran, I Efimov, PCE Moody and EL Raven (2008) Iron Oxidation State Modulates Active Site Structure in a Heme Peroxidase. Biochemistry 47; 4403-4409
CL Metcalfe, IK Macdonald, EJ Murphy, KA Brown, EL Raven & PCE Moody (2008). The tuberculosis prodrug isoniazid bound to activating peroxidases. J. Biol. Chem. 283; 6193-6200
W-C Huang, ACG Westlake, J-D Marechal, MG Joyce, PCE Moody, & GCK Roberts (2007) Filling a hole in cytochrome P450 BM3 improves substrate binding and catalytic efficiency, J. Mol. Biol. 373(3):633-51
I Efimov, ND Papadopoulou, KJ McLean, SK Badyal, I K Macdonald, AW. Munro, PCE Moody & EL Raven (2007) The Redox Properties of Ascorbate Peroxidase, Biochemistry 46; 8017-8023
SK Badyal, MG Joyce, KH Sharp, HE Seward, M Mewies, J Basran, IK Macdonald, PCE Moody & EL Raven (2006) Conformational Mobility in the Active Site of a Heme Peroxidase J. Biol. Chem. 281; 24512-24520.
IK MacDonald, SK Badayl, L Ghamsari, PCE Moody & EL Raven (2006) The interaction of Ascorbate Peroxidase with Substrates: A Mechanistic and Structural Analysis. Biochemistry45; 7808-7817
VE Pye, AP Tingey, RL Robson & PCE Moody (2004) The Structure and Mechanism of Serine Acetyltransferase from Escherichia coli. J. Biol. Chem. 279; 40729-40736
R Pierattelli, L Banci, NAJ Eady, J Bodiguel, JN Jones, PCE Moody, E Lloyd Raven, B Jamart-Grégoire & KA Brown (2004) Enzyme-catalyzed Mechanism of Isoniazid Activation in Class I and Class III Peroxidases J. Biol. Chem. 279; 39000 – 39009
KH Sharp, PCE Moody, KA Brown & E. Lloyd Raven (2004) Crystal Structure of the Ascorbate Peroxidase-Salicylhydroxamic Acid Complex. Biochemistry 43; 8644-8651.
EL Raven, L Lad, KH Sharp, M Mewies & PCE Moody (2004) Defining substrate specificity and catalytic mechanism in ascorbate peroxidase. In Free Radicals: Enzymology, Signalling and Disease pp 27-38. (Ed. CE Cooper, MW Wilson, VM Darley-Usmar) Portland Press
H Khan, T Barna, RJ. Harris, NC. Bruce, I Barsukov, AW Munro, PCE Moody & NS Scrutton, (2004) Atomic Resolution Structures and Solution Behavior of Enzyme-Substrate Complexes of Enterobacter cloacae PB2 Pentaerythritol Tetranitrate Reductase: Multiple conformational states and implications for the mechanism of nitroaromatic explosive degradation J. Biol. Chem. 279; 30563 – 30572
KH Sharp, PCE Moody & E Lloyd Raven, (2003) A new framework for understanding substrate binding and functional diversity in haem peroxidases. Dalton Transactions 22; 4208-4215.
KH Sharp, M Mewies, PCE Moody & E Lloyd Raven, (2003) Crystal structure of the ascorbate peroxidase-ascorbate complex Nature Structural Biology 10; 303-307
H Khan, RJ Harris, T Barna, DH Craig, NC Bruce, AW Munro, Peter CE Moody & NS Scrutton (2002) Kinetic and Structural Basis of Reactivity of Pentaerythritol Tetranitrate Reductase with NADPH, 2-Cyclohexenone, Nitroesters, and Nitroaromatic Explosives J. Biol. Chem. 277; 21906 – 21912
T Barna, HL Messiha, C Petosa, NC. Bruce, NS Scrutton, & PCE Moody (2002) Crystal Structure of Bacterial Morphinone Reductase and Properties of the C191A Mutant Enzyme. J. Biol. Chem. 277; 30976 – 30983
RE Williams, DA Rathbone, PCE Moody, NS Scrutton & NC Bruce, (2001). Degradation of explosives by nitrate ester reductases. Biochem. Soc. Symp. 68 143-153.
LY Lian, CS Allardyce, PCE Moody & GCK Roberts (2001) Structure and folding of glutathione S-transferase A1-1: structural transition and ligand interactions CHEM-BIOL INTERACT 133 (1-3): 13-16
DH Craig, T Barna, PCE Moody, NC Bruce, SK Chapman, AW Munro & NS Scrutton (2001) Effects of environment on flavin reactivity in morphinone reductase: analysis of enzymes displaying differential charge near the N1 atom and C2 carbonyl region of the active site flavin. Biochem. J. 359; 315-323
TM Barna, H Khan, NC Bruce, I Barsukov, NS Scrutton & PCE Moody (2001) Crystal structure of pentaerythritol tetranitrate reductase: "Flipped" binding geometries for steroid substrates in different redox states of the enzyme. J. Mol. Biol. 310; 433-447
JEA Wibley, AE Pegg & PCE Moody (2000) Crystal Structure of the Human O6Alkylguanine-DNA Alkyltransferase. Nucl. Acids Res. 28; 393-401
PE Verdemato JEA Wibley LY Lian & PCE Moody (2000) DNA recognition by O6Alkyguanine-DNA Alkyltransferases. Cold Spring Harbor 65th Symposium on Quantitative Biology “Biological responses to DNA damage” (Ed. B. Stillman)
L Mazzarella, R D'Avino, G di Prisco, C Savino, L Vitagliano, PCE Moody & A Zagari (1999) Crystal structure of Trematomus newnesi haemoglobin re-opens the Root effect question. J. Mol. Biol. 287; 897-906
GN Major, GB Notarianni, SJ Ross, MC Case JA Brannigan, DI Roper, PM Potter, TP Brent, PCE Moody (1999) Evidence for autoproteolysis of substrate-inactivated O-6-methylguanine-DNA methyltransferase following DNA repair. British Journal of Cancer 81; 576
SM Cutfield, GJ Davies, G Murshudov, BF Anderson, PCE Moody, PA Sullivan, & JF Cutfield (1999) The Structure of the Exo-β-(1,3)-Glucanase from Candida albicans in Native and Bound Forms: Relationship between a Pocket and Groove in Family 5 Glycosyl Hydrolases J. Mol. Biol. 294; 771-783
T Barna, PCE Moody, DH Craig, NC Bruce, & NS Scrutton (1999) Structure and mechanism of an explosives-degrading enzyme: PETN reductase . In Flavins and Flavoproteins (Eds. Ghisha, S., Kroneck, P., Macheroux, P. & Sund, H) 671-674
PCE Moody, DH Craig, NS Scrutton, AW Munro, SK Chapman & NC Bruce (1999) Structure and mechanism of an opiate-transforming enzyme: morphinone reductase. In Flavins and Flavoproteins (Eds. Ghisha, S., Kroneck, P., Macheroux, P. & Sund, H) 667-670
RE Williams D Rathbone NC Bruce NS Scrutton, PCE Moody & S Nicklin (1999) The Old Yellow Enzyme family of flavoenzymes – comparison of substrate specificity and activity against explosives. In Flavins and Flavoproteins (Eds. Ghisha, S., Kroneck, P., Macheroux, P. & Sund, H) 663-666
N Chandra, KR Acharya & PCE Moody (1999) Analysis and characterization of data from twinned crystals. Acta Cryst. D55; 1750-1758
PE Verdemato, PCE Moody, LY Lian (1999) Elucidating the binding mechanism of the DNA repair protein Ada-C Frontiers of NMR in Molecular Biology VI Keystone Symposia on Molecular and Cellular Biology
PE Verdemato & PCE Moody (1998) Repair of alkylated DNA by the E. coli Ada protein.Nucleic Acids and Molecular Biology 12; 1-27 (Ed. F. Eckstein & D.M.J. Lilley)
PCE Moody, N Shikotra, CE French, NC Bruce & NS Scrutton (1998) Crystallization and preliminary diffraction studies of pentaerythritol tetranitrate reductase from Enterobacter cloacaePB2. Acta Cryst. D 54; 675-677
SH Done, JA Brannigan, PCE Moody & RE Hubbard (1998) Ligand induced conformational changes in penicillin acylase. J.Mol. Biol 284; 463-475
DH Craig PCE Moody, NC Bruce & NS Scrutton (1998) Reductive and oxidative half-reactions of morphinone reductase from Pseudomonas putida M10: a kinetic and thermodynamic analysis. Biochemistry 37; 7598-7607
JA Rafferty, JEA Wibley, P Speers, I Hickson, GP Margison, PCE Moody, KT Douglas (1997) The potential role of glycine-160 of human O6-alkylguanine-DNA alkyltransferase in reaction with O6-benzylguanine as determined by site-directed mutagenesis and molecular modeling comparisons. BBA -Protein Structure and Molecular Enzymology. 1342; 90-102
PCE Moody, N Shikotra, CE French, NC Bruce & NS Scrutton (1997) Crystallisation and preliminary diffraction studies of morphinone reductase, a flavoprotein involved in the degradation of morphine alkaloids. Acta Cryst. D 53; 619-621
NH Keep, M Barnes, I Barsukov, R Badii, L-Y Lian, AW Segal, PCE Moody & GCK Roberts (1997) A modulator of rho family G proteins, rhoGDI binds these G proteins via an immunoglobulin-like domain and a flexible N-terminal arm. Structure 5; 623-633
GCK Roberts, NH Keep, M Barnes, I Barsukov, R Badii, LY Lian, AW Segal & PCE Moody (1997) The structure of rho-GDI and its interaction with the small GTPase RAC FASEB Journal 11; 3424
SM Dunn, PCE Moody, JA Downie & WV Shaw. (1996) Crystallization and preliminary diffraction studies of Nodl, a rhizobial O-acetyl-transferase involved in the host-specific nodulation of legume roots. Prot. Sci. 5; 538-541
JEA Wibley, JH Mckie, K Embrey, DS Marks, KT Douglas, MH Moore & PCE Moody (1995) A homology model of the 3-dimensional structure of human O-6-alkylguanine-DNA alkyltransferase based on the crystal-structure of the C-terminal domain Of the Ada protein from Escherichia coli. Anti-Cancer Drug Design 10; 75-95
JL Whittingham, S Chaudhuri, EJ Dodson, PCE Moody & GG Dodson (1995) X-ray crystallographic studies on hexameric insulins in the presence of helix-stabilizing agents, thiocyanate, methylparaben, and phenol. Biochemistry 34; 15553-15563
HJ Duggleby, SP Tolley, CP Hill, EJ Dodson, G Dodson & PCE Moody (1995) Penicillin acylase has a single amino-acid catalytic centre. Nature 373; 264-268
SM Cutfield, EJ Dodson, BF Anderson, PCE Moody, CJ Marshall, PA Sullivan, JF Cutfield (1995) The crystal structure of a major secreted aspartic proteinase from Candida albicans in complexes with 2 inhibitors. Structure 3; 1261-1271
PCE Moody & MH Moore (1995) Crystal Structure of E. coli O6-Methylguanine-DNA methyltransferase. Contributions to Oncology 49; 16-24 Karger Press
JA Brannigan, G Dodson, HJ Duggleby, PCE Moody, JL Smith, DR Tomchick, AG Murzin (1995) A protein catalytic framework with an N-terminal nucleophile is capable of self-Activation. Nature 378; 416-419
MH Moore, JM Gulbis, EJ Dodson, B Demple, PCE Moody (1994) Crystal structure of a suicidal DNA-repair protein - The Ada O-6-methylguanine-DNA methyltransferase from Escherichia coli. EMBO J. 13; 1495-1501
G Laughlan, AIH Murchie, DG Norman, MH Moore, PCE Moody, DMJ Lilley & B Luisi (1994) The high-resolution crystal structure of a parallel-stranded guanine tetraplex. Science 265; 520-524
G Lange, SJ Lewis, GN Murshudov, GG Dodson, PCE Moody, JP Turkenburg, AN Barclay, RL Brady (1994) Crystal structure of an extracellular fragment of the rat Cd4 receptor-containing domain-3 and domain-4. Structure 2; 469-481
EJ Dodson, GG Dodson, RE Hubbard, PCE Moody, J Turkenburg, J Whittingham, B Xiao, J Brange, N Kaarsholm, & H Thogersen (1993) Insulin Assembly - Its modification by protein engineering and ligand-binding. Phil. Trans. Royal Soc. (London) A 345; 153-164
S Cutfield, C Marshall, P Moody, P Sullivan, J Cutfield (1993) Crystallization of inhibited aspartic proteinase from Candida albicans. J. Mol. Biol. 234; 1266-1269
PCE Moody & AJ Wilkinson (1991) "Protein Engineering - In Focus", (Series Ed. D. Rickwood) IRL-OUP, Oxford
MR Gibbs, PCE Moody, AGW Leslie (1990) Crystal structure of the aspartic-acid-199-asparagine mutant of chloramphenicol acetyltransferase to 2.35-Å Resolution - structural consequences of disruption of a buried salt bridge. Biochemistry 29; 11261-11265
PCE Moody & B Demple (1988) Crystallization of O-6-Methylguanine-DNA methyltransferase from Escherichia coli. J. Mol. Biol. 200; 751-752
AGW Leslie, PCE Moody & WV Shaw (1988) Structure of chloramphenicol acetyltransferase at 1.75-Å resolution. Proc. Natl. Acad. Sci. (USA). 85; 4133-4137
T Skarzynski, PCE Moody, AJ Wonacott (1987) Structure of holo-glyceraldehyde-3-phosphate dehydrogenase from Bacillus Stearothermophilus at 1.8 Å Resolution. J. Mol. Biol. 193; 171-187
AGW Leslie, AJ Wonacott, & PCE Moody (1984). Crystal-Structure Refinement of Apo and Partially Liganded Glyceraldehyde-3-Phosphate Dehydrogenase (GAPDH) at 4 Å Resolution. Acta Cryst. A 40: C18-C18
PCE Moody & AJ Wonacott (1984). Substrate Binding in D-Glyceraldehyde 3-Phosphate Dehydrogenase - a Revised Model. Acta Cryst. A 40: C26-C2
PCE Moody (1984) Structural studies of the active site and catalytic function of glyceraldehyde-3-phosphate dehydrogenase PhD Thesis Imperial College London https://spiral.imperial.ac.uk:8443/bitstream/10044/1/37253/2/Moody-PCE-1984-PhD-Thesis.pdf

Research

Research is documented in my LISCB Page.

Supervision

My interests are in using structure to understand enzyme mechanism, particularly of redox enzymes and the enzymes of the glycolytic/gluconeogenic axis in enteric pathogens. I am keen to expand the methods used, especially to study the structures of enzyme intermediates. This may include developing neutron crystallography, dynamic crystallography with synchrotrons or X-ray free electron lasers.

Research also takes place at synchrotrons (Diamond Light Source, ESRF in Grenoble), neutron sources (ILL in Grenoble, FRM-II in Munich, ONRL in USA) and Free Electron Lasers (SACLA in Japan, EuXFEL in Hamburg).