8BRK

Room temperature crystal structure of cytochrome c' from Thermus thermophilus

8BRK の概要

• エントリーDOI: 10.2210/pdb8brk/pdb
• 分子名称: Probable cytochrome, HEME C (3 entities in total)
• 機能のキーワード: heme protein, diatomic gas binding protein, electron transfer, electron transport
• 由来する生物種: Thermus thermophilus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 15560.63

構造登録者

Fujii, S.,Hough, M.A. (登録日: 2022-11-23, 公開日: 2023-05-24, 最終更新日: 2024-10-23)

主引用文献

Mikolajek, H.,Sanchez-Weatherby, J.,Sandy, J.,Gildea, R.J.,Campeotto, I.,Cheruvara, H.,Clarke, J.D.,Foster, T.,Fujii, S.,Paulsen, I.T.,Shah, B.S.,Hough, M.A.
Protein-to-structure pipeline for ambient-temperature in situ crystallography at VMXi.
Iucrj, 10:420-429, 2023

PubMed Abstract: The utility of X-ray crystal structures determined under ambient-temperature conditions is becoming increasingly recognized. Such experiments can allow protein dynamics to be characterized and are particularly well suited to challenging protein targets that may form fragile crystals that are difficult to cryo-cool. Room-temperature data collection also enables time-resolved experiments. In contrast to the high-throughput highly automated pipelines for determination of structures at cryogenic temperatures widely available at synchrotron beamlines, room-temperature methodology is less mature. Here, the current status of the fully automated ambient-temperature beamline VMXi at Diamond Light Source is described, and a highly efficient pipeline from protein sample to final multi-crystal data analysis and structure determination is shown. The capability of the pipeline is illustrated using a range of user case studies representing different challenges, and from high and lower symmetry space groups and varied crystal sizes. It is also demonstrated that very rapid structure determination from crystals in situ within crystallization plates is now routine with minimal user intervention.

PubMed: 37199504
DOI: 10.1107/S2052252523003810

実験手法

X-RAY DIFFRACTION (1.75 Å)