4YCR

Structure determination of an integral membrane protein at room temperature from crystals in situ

4YCR の概要

• エントリーDOI: 10.2210/pdb4ycr/pdb
• 関連するPDBエントリー: 3M71
• 分子名称: Tellurite resistance protein TehA homolog, octyl beta-D-glucopyranoside (3 entities in total)
• 機能のキーワード: in situ data collection, membrane protein, multiple datasets, synchrotron beamline
• 由来する生物種: Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
• 細胞内の位置: Cell inner membrane ; Multi- pass membrane protein : P44741
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 34052.11

構造登録者

Axford, D.,Hu, N.J.,Foadi, J.,Choudhury, H.G.,Iwata, S.,Beis, K.,Evans, G.,Alguel, Y. (登録日: 2015-02-20, 公開日: 2015-06-03, 最終更新日: 2024-05-08)

主引用文献

Axford, D.,Foadi, J.,Hu, N.J.,Choudhury, H.G.,Iwata, S.,Beis, K.,Evans, G.,Alguel, Y.
Structure determination of an integral membrane protein at room temperature from crystals in situ.
Acta Crystallogr.,Sect.D, 71:1228-1237, 2015

PubMed Abstract: The structure determination of an integral membrane protein using synchrotron X-ray diffraction data collected at room temperature directly in vapour-diffusion crystallization plates (in situ) is demonstrated. Exposing the crystals in situ eliminates manual sample handling and, since it is performed at room temperature, removes the complication of cryoprotection and potential structural anomalies induced by sample cryocooling. Essential to the method is the ability to limit radiation damage by recording a small amount of data per sample from many samples and subsequently assembling the resulting data sets using specialized software. The validity of this procedure is established by the structure determination of Haemophilus influenza TehA at 2.3 Å resolution. The method presented offers an effective protocol for the fast and efficient determination of membrane-protein structures at room temperature using third-generation synchrotron beamlines.

PubMed: 26057664
DOI: 10.1107/S139900471500423X

実験手法

X-RAY DIFFRACTION (2.3 Å)