Cryo-crystallography was the driving force of structural biology, literally deciphering the structures of life. The integrated knowledge has informed powerful machine learning technologies to not only solve the folding problem but to imagine new proteins, some of which are even functional. However, protein function is often dominated by small kinetic barriers that are not easily predicted....
(representing the entire SSRL-SMB team)
Structural Molecular Biology (SMB), Stanford Synchrotron Radiation Lightsource (SSRL), SLAC National Accelerator Laboratory, Stanford University, Menlo Park, United States of America
Structural biologists are undertaking increasingly challenging projects including the study of membrane proteins and complex multi-component machines. Structural...
P11 at PETRA III (DESY, Hamburg) is a high-throughput instrument for macromolecular crys-
tallography [1]. The beamline has tuneable photon energy between 5.5 - 28 keV and and beam
sizes from 200 x 200 μm to 4 x 9 μm2 can be used with a maximum photon flux of 1x1013 ph/s at
12 keV energy. Equipped with a fast detector Eiger2 X 16M as the stationary detector (max 133 Hz),
this high flux...
Microbial rhodopsins constitute a large superfamily of light-sensitive membrane proteins, which are vital for numerous microorganisms on Earth, and for 20 years also being most-actively used in neuroscience and medicine in the biotechnology named optogenetics. The major role for optogenetics is played by ion-transporting rhodopsins. Understanding of their molecular mechanisms of functioning...
Abstract: Enzyme catalysis is essential for life and is a central phenomenon in biochemistry. The advent of time-resolved serial crystallography, initially enabled by X-ray free electron lasers (XFELs) and now expanding to synchrotron X-ray sources, allows enzyme catalysis to be observed catalysis in real time, in near-physiological conditions, and at atomic resolution. I will describe our...
There is increasing interest in obtaining room temperature, time resolved crystal structures of
proteins carrying out their biological functions. The transition between conventional cryogenic
macromolecular crystallography and serial crystallography involving microcrystals remains chal-
lenging for many projects. We have recently demonstrated the capability to measure good quality,
low dose...
