6FMR

IMISX-EP of Se-PepTSt

6FMR の概要

• エントリーDOI: 10.2210/pdb6fmr/pdb
• 分子名称: Di-or tripeptide:H+ symporter, (2S)-2,3-DIHYDROXYPROPYL(7Z)-PENTADEC-7-ENOATE, PHOSPHATE ION, ... (4 entities in total)
• 機能のキーワード: serial crystallography, experimental phasing, in meso crystallization, in situ diffraction data collection, membrane protein structure., transport protein
• 由来する生物種: Streptococcus thermophilus (strain ATCC BAA-250 / LMG 18311)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 58136.28

構造登録者

Huang, C.-Y.,Olieric, V.,Howe, N.,Warshamanage, R.,Weinert, T.,Panepucci, E.,Vogeley, L.,Basu, S.,Diederichs, K.,Caffrey, M.,Wang, M. (登録日: 2018-02-02, 公開日: 2018-08-29, 最終更新日: 2018-10-10)

主引用文献

Huang, C.Y.,Olieric, V.,Howe, N.,Warshamanage, R.,Weinert, T.,Panepucci, E.,Vogeley, L.,Basu, S.,Diederichs, K.,Caffrey, M.,Wang, M.
In situ serial crystallography for rapid de novo membrane protein structure determination.
Commun Biol, 1:124-124, 2018

PubMed Abstract: De novo membrane protein structure determination is often limited by the availability of large crystals and the difficulties in obtaining accurate diffraction data for experimental phasing. Here we present a method that combines in situ serial crystallography with de novo phasing for fast, efficient membrane protein structure determination. The method enables systematic diffraction screening and rapid data collection from hundreds of microcrystals in in meso crystallization wells without the need for direct crystal harvesting. The requisite data quality for experimental phasing is achieved by accumulating diffraction signals from isomorphous crystals identified post-data collection. The method works in all experimental phasing scenarios and is particularly attractive with fragile, weakly diffracting microcrystals. The automated serial data collection approach can be readily adopted at most microfocus macromolecular crystallography beamlines.

PubMed: 30272004
DOI: 10.1038/s42003-018-0123-6

実験手法

X-RAY DIFFRACTION (2.7 Å)