BioMAX is the first X-ray macromolecular crystallography beamline of MAX IV Laboratory, which is in user operations since 2017. It is a state-of-the-art resource accommodating multiple cutting edge experimental possibilities. The design goal for BioMAX was to create a stable and reliable beamline that is user friendly. The beamline experiment set-up is highly automated, in terms of both sample handling hardware and data analysis, including feedback on the data collection.
The X-ray beam focus is 20 x 5 μm2 at the sample position with a photon flux of 2 x 1013 ph/s at 500 mA ring current. The operational energy range of the beamline is 5–25 keV. Alternatively, using aperture overfilling it is possible to obtain a stable 5 x 5 μm2 beam at the sample position. Due to its extensive energy tunability, BioMAX is an ideal source for de novo phasing using the anomalous signal of heavy elements. Beam defocusing creates a practically parallel beam, which can be used to resolve extremely large unit cells > 1000 Å at high resolution. Due to its small beam cross-section and optional parallel beam, BioMAX is an optimal experimental set-up for X-ray crystallography using microcrystals and ultra large unit cells. Initial synchrotron based serial crystallography (SSX) experiments using an High-Viscosity-Extrusion injector designed and built by Bruce Doak (MPI-Heidelberg) have been carried out.
|Available for||Technique description|
|General Users||Data collection at fixed energy between 6 and 24 keV, detector distance between 126 and 900 mm, beam focus of 20x5 microns, 50x50 microns or 100x100 microns and defining aperture of 5, 10, 20, 50 and 100 microns.|
|General Users||Automated sample mounting and dismounting from UniPucks, 29 puck positions in dewar.|
|General Users||Sample temperature 100 K; room temperature with or without humidity control available for manual mounting only.|
|General Users||SAD and MAD experiments.|
|General Users||Automated data integration, scaling and merging. Offline remote access for manual data processsing.|
|General Users||Serial crystallography experiments using HVE-injector (High viscosity extrusion injector), fixed target scan using the MD3. Please contact beamline manager.|
|General Users||Element identification by X-ray Fluorescence.|
|General Users||Remote data collection.|
|General Users||Fragment-based drug screening. Please contact beamline manager.|
|See also BioMAX User Information|
Structures of several clinically relevant NUDT15 variants are discovered – paving the way for better cancer treatments
NUDT15 bound to TH7755. Credit: Emma Scaletti Recent research by a group of researchers from Sweden, the US, and the UK successfully developed a specific NUDT15 inhibitor, TH7755, that helped the group to obtain structures of clinically relevant NUDT15 variants: Arg139Cys, Arg139His, Val18Ile, and V18_V19insGlyVal. These insights allow further understandings of the structural basis of