7AYS

Structure of bovine trypsin determined from single femtosecond snapshots per orientation at room temperature

7AYS の概要

• エントリーDOI: 10.2210/pdb7ays/pdb
• 分子名称: Cationic trypsin, BENZAMIDINE, SULFATE ION, ... (5 entities in total)
• 機能のキーワード: serine protease, hydrolase
• 由来する生物種: Bos taurus (cattle)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 23580.58

構造登録者

Jensen, M. (登録日: 2020-11-13, 公開日: 2021-01-20, 最終更新日: 2026-03-04)

主引用文献

Jensen, M.,Ahlberg Gagner, V.,Cabello Sanchez, J.,Bengtsson, A.U.J.,Ekstrom, J.C.,Bjorg Ulfarsdottir, T.,Garcia-Bonete, M.J.,Jurgilaitis, A.,Kroon, D.,Pham, V.T.,Checcia, S.,Coudert-Alteirac, H.,Schewa, S.,Rossle, M.,Rodilla, H.,Stake, J.,Zhaunerchyk, V.,Larsson, J.,Katona, G.
High-resolution macromolecular crystallography at the FemtoMAX beamline with time-over-threshold photon detection.
J.Synchrotron Radiat., 28:64-70, 2021

PubMed 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 intensity distribution compared with theoretical distribution, I/σ, R/R and CC statistics versus resolution. The FemtoMAX beamline provides an interesting alternative to X-ray free-electron lasers when studying reversible processes in protein crystals.

PubMed: 33399553
DOI: 10.1107/S1600577520014599

実験手法

X-RAY DIFFRACTION (2.1 Å)