Macromolecular Crystallography (MX)
MX is a core activity at Diamond with seven beamlines dedicated to the technique alongside the XFEL Hub, Membrane Protein Laboratory and XChem fragment screening facility for the extensive UK structural biology community as well as researchers in Europe and beyond. The staff of the MX group are recognised as innovative world leaders in MX, moving the goalposts of what is feasible for 'conventional' MX as well as developing techniques and beamlines that transform MX to the next level, enabling new experiments and methodologies. The group takes a long term approach to enabling new capabilities at its suite of beamlines to meet the current and future demands of an exacting community of scientists; in 2017 this was no different, as can be seen by the exciting developments here.
I02-1 VMXmUnder construction
VMXm is a micro/nanofocus MX beamline aimed at atomic structure determination in cases where the production of significant quantities of protein material and crystals is problematic.More information
Wavelength: 0.57 - 2.0 Å
Energy: 7.0 - 25.0 keV
The Versatile Macromolecular X-tallography in-situ (VMXi) beamline will be an entirely automated facility for characterisation of, and data collection directly from, crystallisation experiments in situ.More information
Energy: 12 keV
High throughput and highly automated beamline for optimised MAD and SAD experiments. Capable of accepting CL3 type experiments on crystals of pathogens.More information
Detector: Eiger2 XE 16M
Wavelength: 0.5 - 2.5 Å
I04 Microfocus MX
Variable focus from 5 to 100 microns, high throughput and highly automated beamline for optimised MAD and SAD experiments.More information
Detector: Eiger2 XE 16M
Wavelength: 0.69 - 2.07 Å
I04-1 Fixed wavelength MX
High throughput and highly automated fixed wavelength SAD beamline for macromolecular crystallography.More information
Detector: Pilatus 6M-F
Wavelength: 0.92Å (fixed)
I23 Long-Wavelength MXCommissioning
A unique facility for solving the crystallographic phase problem, using the small anomalous signals from sulphur or phosphorous which are present in native protein or RNA/DNA crystals. Additionally, anomalous difference Fourier maps can be used to locate sulphur and phosphorous positions to assist model building at low resolution and/or identify lighter atoms such as chlorine, potassium and calcium.More information
Energy: 2.1 – 11 keV
I24 Microfocus MX
High throughput variable microfocus beamline for optimised MAD and SAD experiments on crystals down a few microns in size.More information
Detector: Pilatus3 6M
Wavelength: 0.62Å - 1.77Å
Membrane Protein Laboratory
The Membrane Protein Lab (MPL) at Diamond is a research and training facility for scientists interested in solving the 3D structures of membrane proteins by X-ray crystallography.More information
The UK is taking a leading role in the development of a new structural biology facility (SFX) at the European X-ray Free Electron Laser (XFEL), in Hamburg, Germany, and a complementary facility at Diamond (The UK XFEL Hub) to help develop the required expertise.More information
Specialised high flux microfocus beams for microcrystal data collection or the illumination of subvolumes of larger inhomogeneous crystals.More information...
The highly automated beamlines enable data collection from anywhere in the world via remote access. Systems are in place for shipping samples to and from Diamond Light Source. New users can borrow pucks and tools.More information...
In situ Data Collection
In situ data collection and sample characterization directly from crystals in their crystallization plates.More information...
Sample Humidity Control
Control of the sample crystal's relative humidity with the aim of improving diffraction quality through improved packing of protein molecules constituting the lattice.More information...
On-line and off-line UV-Vis spectroscopy of macromolecular samples to study enzyme reaction mechanisms and radiation damage.More information...
Crystal reorientation to optimize data collection strategies for anomalous diffraction data collection and low symmetry spacegroups, or very long axis unit cells.More information...
All beamlines are designated bio containment level 1. For containment level 2 samples beamlines I03 and I24 can be used and beamline I03 can be configured to run at biocontainment level 3.More information...
|Wavelength range (Å) ||0.6 - 2.3||0.69 - 2.07||0.92 (fixed)||0.7 - 2.0|
|Energy range (keV) ||5.2 - 21.0||6.0 - 18.0||13.5 (fixed)||6.4 - 20.0|
|Default settings (Å/keV)||0.98 / 12.7||0.98 / 12.66||0.92 / 13.53||0.97 / 12.8|
|Flux (ph/s) in full beam at default energy at 300 mA||1.7 x 1012||2.8 x 1011||9.0 x 1011||3.0 x 1012|
|Default beamsize (µm)||90 x 20||30 x 20||60 x 50||8 x 8|
|Full beam size at sample (µm)||90 x 20 90 x 30 100 x100 55 x 10||10 x 5 --> 110 x 100||60 x 50|| |
5 x 5 --> 50 x 40
|Available apertures (µm)|| |
20, 50, 100
|10, 20, 30, 50 and 70|
|Detectors (Dectris type)|| |
Eiger2 XE 16M
Eiger2 XE 16M
|Number of unipucks / SPINE pins||37/592||37 / 592||37 / 592||37 / 592|
|Maximum samples / hour||30||30||30||30|
|Typical samples / hour||15 - 25||15 - 25||15 - 35||15 - 25|
Reserve access well ahead of your visit either at the links in the web page or via your local contact to facilities such as
Understand the visit timings you are scheduled for.
Refer to the manual for data collection possibilities –