9EWK

Solvent organization in ultrahigh-resolution protein crystal structure at room temperature

9EWK の概要

• エントリーDOI: 10.2210/pdb9ewk/pdb
• 分子名称: Crambin, ETHANOL (3 entities in total)
• 機能のキーワード: crambin, plant protein
• 由来する生物種: Crambe hispanica subsp. abyssinica
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 4820.55

構造登録者

Chen, J.C.-H.,Gilski, M.,Chang, C.,Borek, D.,Rosenbaum, G.,Lavens, A.,Otwinowski, Z.,Kubicki, M.,Dauter, Z.,Jaskolski, M.,Joachimiak, A. (登録日: 2024-04-04, 公開日: 2024-09-04, 最終更新日: 2024-11-06)

主引用文献

Chen, J.C.H.,Gilski, M.,Chang, C.,Borek, D.,Rosenbaum, G.,Lavens, A.,Otwinowski, Z.,Kubicki, M.,Dauter, Z.,Jaskolski, M.,Joachimiak, A.
Solvent organization in the ultrahigh-resolution crystal structure of crambin at room temperature.
Iucrj, 11:649-663, 2024

PubMed Abstract: Ultrahigh-resolution structures provide unprecedented details about protein dynamics, hydrogen bonding and solvent networks. The reported 0.70 Å, room-temperature crystal structure of crambin is the highest-resolution ambient-temperature structure of a protein achieved to date. Sufficient data were collected to enable unrestrained refinement of the protein and associated solvent networks using SHELXL. Dynamic solvent networks resulting from alternative side-chain conformations and shifts in water positions are revealed, demonstrating that polypeptide flexibility and formation of clathrate-type structures at hydrophobic surfaces are the key features endowing crambin crystals with extraordinary diffraction power.

PubMed: 39190507
DOI: 10.1107/S2052252524007784

実験手法

X-RAY DIFFRACTION (0.7 Å)