Crystallography Facilities

The Department has excellent facilities for macromolecular crystallography including the powerful X-ray generator & CCD detector along with robotics for crystal growth and visualisation. The laboratory's interests are wide and range from proteins involved in transcription factors, cell signalling and cellular adhesion to redox enzymes involved in drug action.

 

X-ray crystallography data collection in-house uses our Rigaku 007HF generator and Saturn 944+ CCD detector mounted on an AFC-10 K 4-circle goniometer, equipped with an Oxford Cryosystems series 700 Cryostream.

Contact: Professor Peter Moody

 

The other port of the X-ray generator  is fitted with an Raxis-IV modified to include a single-crystal spectrophotometer (Optique Peter lenses fibre-optic coupled to a W/D lightsource and Ocean Optics MayaPro 2000)

 

Beside using our in-house X-ray equipment (link), we collect X-ray data at synchrotrons such as Diamond Light Source and ESRF

Selected Recent Publications:

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) DOI:10.1038/ncomms13445 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 DOI:10.1107/S2059798316016314

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  DOI: 10.1126/science.1254398.  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

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Contact Details

Department of Molecular and Cell Biology
Henry Wellcome Building
Lancaster Road
Leicester
LE1 7RH (Postal)

LE1 7HB (Sat Nav/Online maps)

T:  +44(0)116 229 7038
F:  +44(0)116 229 7123
MolCellBiol@le.ac.uk

Accessibility

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Redfearn Lecture 2017

To Be Confirmed