Protein structure

Protein structure

X-Ray crystallography utilises X-ray diffraction by single protein crystals to elucidate three dimensional structures at atomic resolution. The technique plays a pivotal role in understanding how individual amino acids interact with small molecule ligands and cofactors.

The MPSF (Manchester Protein Structure Facility) provides a complete service pipeline, taking you from purified protein to crystal structure. The MPSF is serviced by two full time senior experimental officers. Expert users can gain access to the facility equipment, whilst non experts are offered a complete service pipeline for structure elucidation.

Meeting the often rate limiting challenge of crystallogenesis are two complementary high throughput nanolitre dispensing robots (Mosquito & Phoenix) allowing rapid screening and optimisation. The facility also houses two rotating anode X-ray generators and associated data collection equipment. These in-house facilities are further supplemented with regular synchrotron access.

All services and equipment are available to both University of Manchester researchers and external users (academic & commercial).


Dr Colin Levy ¦ ¦ Tel: +44 (0)161 275 5090


The facility is actively involved in a wide range of research topics across several faculties and has contributed to a number of publications in a broad range of journals.


The standard access point to the MPSF is purified protein, however technical support can be provided to help you achieve this goal. If you are thinking of determining a crystal structure then the time to talk to the MPSF is now.

The MPSF provides an efficient and streamlined approach to protein crystallography. Complete crystal growth, characterisation, data collection and subsequent structure determination services are available.

For assistance with Protein Production

Dr Edward McKenzie | | +44 (0)161 257 5617

For assistance with Biomolecular Analysis including MALS analysis

Dr Thomas A. Jowitt | | +44 (0)161 306 5176



To meet the challenge of this rate limiting step two complementary robotic systems (Mosquito & Phoenix) enable the rapid and reproducible creation of crystal trials. Both capable of nanolitre dispensing, broad screening and optimisation experiments are rapidly carried out consuming minimal quantities of protein.

Experimental crystallisation plates may be incubated at a variety of temperatures in either a dedicated cold room housed within the facility or using one of two incubators. More sophisticated temperature screening is available through the use of two TG-40 temperature control units.

A Belle Technology glove box provides an anaerobic environment for all aspects of crystallogenesis and sample preparation. Samples grown under anaerobic conditions can be cryocooled within the box prior to transfer for diffraction data collection either in-house or at a synchrotron facility.

Plates are inspected using one of three Nikon SMZ 1000 microscopes (2 with camera facilities) or with an Art Robbins CrysCam visualisation system. An aditional Nikon SMZ 1000 microscope is located within the cold room for inspecting temperature sensitive samples.


A microspectrophotometer from 4DX Systems AB is available to acquire absorption spectra measurements from single crystals in the UV-VIS-NIR spectral range. A dedicated Oxford cryosystems cold head allows exquisite temperature control at the sample. The cold head is fitted with an in-house designed cryo shutter allowing flash freezing for cryo trapping experiments.

X-Ray Diffraction

The facility houses both a Bruker Microstar microfocus X-ray source and a Rigaku Micromax 007. In addition to the exceptional flexibility this dual setup affords us, we are able to exploit the Rigaku vertical Phi arrangement to couple the 4DX microspec system directly into the X-Ray setup allowing X-ray and spectroscopic data collection from a single crystal.

“…crystal structures are crucial to our interdisciplinary programs focusing on enzyme mechanism and catalysis. The MPSF has, and continues to play a major role in structure determination in our programmes on enzyme catalysed H-transfer, cofactor chemistry and in developing physical models for catalysis.”

Professor Nigel S. Scrutton, Professor of Molecular Enzymology