“BioMAX serial crystallography setup using a High Viscosity Extrusion
(HVE) injector specially designed for the BioMAX endstation by Bruce
Doak of the Max Planck Institute for Medical Research, Heidelberg, and
fabricated at that institute.”
BioMAX has successfully performed the first serial crystallography experiments at the beamline. This new method is performed at room temperature which allows structural biologists to study their molecules at more biologically relevant conditions. The technique can also be used on smaller crystals which will alleviate some of the restrictions for molecules such as membrane proteins, that do not typically form large crystals. Eventually, it is hoped that this technique will allow users at the BioMAX and MicroMAX beamlines to take snapshots of the dynamic states of proteins in rapid succession giving a dynamic view of protein movement and activity.
The serial crystallography technique promises to be very useful to users of both synchrotrons and XFELs. Over the course of one experiment, users were able to measure between 20 and 50 crystals every second, resulting in 20 TB of data from just 3 proteins. BioMAX hopes to quickly master this complex technique in order to offer it to users as soon as possible. It also gives us a glimpse of what will be possible at the newly funded MicroMAX beamline.
In order to start with serial crystallography, BioMAX teamed up with the Schlichting group at MPI Heidelberg. There, Bruce Doak designed the HVE- injector and produced this unique device to match full compatibility to the BioMAX experimental setup successfully. The MPI experts later helped Anastasya Shilova, the BioMAX scientist in charge of this project, to perform the proof-of-principle experiment at MAXIV which made the first user experiment with the Bränden/Neutze group from Göthenburg possible.
While it is too early to comment on the results, the team is excited. The Bränden/Neutze collaboration is scientifically, the highest ranked proposal in all 3 user calls for the BioMAX beamline and the data collection went well. They used a high viscosity extrusion injector to quickly pass protein crystals in front of the MAX IV X-ray beam. To keep the crystals in place and stable at the ambient temperatures, they were embedded in a thick grease which was extruded at high pressure through a 100 µm glass capillary. The team was investigating the cytochrome oxidase protein which is a protein that converts atmospheric oxygen into a for that can be used by human cells. Until recently, it has not been possible to look at this process dynamically, but the team has carried out some pioneering experiments on XFELs in the USA and Japan in order to understand the nature of the chemical reactions carried out by the enzyme. By coming to MAX IV, and establishing serial crystallography, the hope is that the group will be able to do similar experiments to those done at the XFEL which will save time and allow for better optimization of the experimental setup, as well as performing time-resolved experiments in the millisecond range.