High-resolution macromolecular crystallography at the FemtoMAX beamline with time-over-threshold photon detection.

ABSTRACT: Protein dynamics contribute to protein function on different time scales. Ultrafast X-ray diffraction snapshots can visualize the location and amplitude of atom displacements after perturbation. Since amplitudes of ultrafast motions are small, high-quality X-ray diffraction data is necessary for detection. Diffraction from bovine trypsin crystals using single femtosecond X-ray pulses was recorded at FemtoMAX, which is a versatile beamline of the MAX IV synchrotron. The time-over-threshold detection made it possible that single photons are distinguishable even under short-pulse low-repetition-rate conditions. The diffraction data quality from FemtoMAX beamline enables atomic resolution investigation of protein structures. This evaluation is based on the shape of the Wilson plot, cumulative

SUBMITTER: Jensen M 

PROVIDER: S-EPMC7842217 | biostudies-literature | 2021 Jan

REPOSITORIES: biostudies-literature