Crystallisation & X‑Ray

The Crystallisation and X-ray facilities support macromolecular crystallography at the LMB. These facilities provide guidance on the requirements for protein samples to crystallise, through to the determination and analysis of crystal structures.

Protein X-ray crystallography was invented during the early days of the LMB and uses X-ray diffraction patterns to determine the 3D arrangement of the atoms making up the crystals. Given that biological macromolecules can contain very many atoms, specialised methods are needed, including very powerful X-ray beams from synchrotrons and computer algorithms that allow large structures to be determined.

The Crystallisation facility, led by Fabrice Gorrec, provides a large selection of initial screens in pre-filled MRC crystallisation plates, along with optimised robotic liquid handler protocols including nanolitre dispensing on the Mosquito (SPT Labtech).

The X-ray facility, led by Dom Bellini, enables diffraction screening of crystals using in-house Rigaku-MarDTB systems, including an FR-E+ generator, remote data collection at the Diamond Light Source synchrotron and structure determination.

In addition to providing services to LMB scientists, the facilities are also developing new approaches to crystallisation and crystal structure analysis.

The LMB’s YouTube channel has more information about protein crystallisation and crystallography.

Information for the LMB crystallisation facility can be found here.