Peter Moody

Personal Details

Peter MoodyProfessor of Structural Biology

Peter Moody Headshot 2.0

DepartmentMolecular and Cell Biology
Telephone: +44 (0)116 229 7097
Emailpeter.moody@le.ac.uk
Address: Lancaster Rd, LE1 7HB
Web Links: 

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

  1. 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
  2. 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
  3. 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)
  4. PCE Moody & EL Raven (2018) The Nature & Reactivity of Ferryl Heme in Compounds I and II Acc. Chem Res.
  5. 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.
  6. 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
  7. H Kwon, O Smith, EL Raven & PCE Moody (2017) Combining X-ray and Neutron Crystallography with Spectroscopy. Acta Cryst D72 141- 147
  8. 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
  9. 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
  10. 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
  11. 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)
  12. 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
  13. 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.
  14. 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
  15. 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
  16. 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
  17. 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
  18. 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
  19. 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
  20. 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
  21. 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
  22. 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
  23. 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
  24. 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.
  25. 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
  26. 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
  27. 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
  28. 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
  29. 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
  30. 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
  31. 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
  32. 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
  33. 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
  34. 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
  35. 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.
  36. 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
  37. 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
  38. 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
  39. KH Sharp, PCE Moody, KA Brown & E. Lloyd Raven (2004) Crystal Structure of the Ascorbate Peroxidase-Salicylhydroxamic Acid Complex. Biochemistry 43; 8644-8651.
  40. 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
  41. 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
  42. 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.
  43. KH Sharp, M Mewies, PCE Moody & E Lloyd Raven, (2003) Crystal structure of the ascorbate peroxidase-ascorbate complex Nature Structural Biology 10; 303-307
  44. 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
  45. 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
  46. RE Williams, DA Rathbone, PCE Moody, NS Scrutton & NC Bruce, (2001). Degradation of explosives by nitrate ester reductases. Biochem. Soc. Symp. 68 143-153.
  47. 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
  48. 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
  49. 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
  50. JEA Wibley, AE Pegg & PCE Moody (2000) Crystal Structure of the Human O6Alkylguanine-DNA Alkyltransferase. Nucl. Acids Res. 28; 393-401
  51. 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)
  52. 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
  53. 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
  54. 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
  55. 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
  56. 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
  57. 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
  58. N Chandra, KR Acharya & PCE Moody (1999) Analysis and characterization of data from twinned crystals. Acta Cryst. D55; 1750-1758
  59. 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
  60. 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)
  61. 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
  62. SH Done, JA Brannigan, PCE Moody & RE Hubbard (1998) Ligand induced conformational changes in penicillin acylase. J.Mol. Biol 284; 463-475
  63. 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
  64. 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
  65. 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
  66. 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
  67. 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
  68. 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
  69. 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
  70. 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
  71. 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
  72. 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
  73. PCE Moody & MH Moore (1995) Crystal Structure of E. coli O6-Methylguanine-DNA methyltransferase. Contributions to Oncology 49; 16-24 Karger Press
  74. 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
  75. 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
  76. 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
  77. 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
  78. 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
  79. 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
  80. PCE Moody & AJ Wilkinson (1991) "Protein Engineering - In Focus", (Series Ed. D. Rickwood) IRL-OUP, Oxford
  81. 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
  82. PCE Moody & B Demple (1988) Crystallization of O-6-Methylguanine-DNA methyltransferase from Escherichia coli. J. Mol. Biol. 200; 751-752
  83. AGW Leslie, PCE Moody & WV Shaw (1988) Structure of chloramphenicol acetyltransferase at 1.75-Å resolution. Proc. Natl. Acad. Sci. (USA). 85; 4133-4137
  84. 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
  85. 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
  86. PCE Moody & AJ Wonacott (1984). Substrate Binding in D-Glyceraldehyde 3-Phosphate Dehydrogenase - a Revised Model. Acta Cryst. A 40: C26-C2
  87. 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).

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Department of Molecular and Cell Biology

T: +44(0)116 229 7038
E: MolCellBiol@le.ac.uk

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