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6FMT

IMISX-EP of Hg-BacA Soaking SAD

6FMT の概要
エントリーDOI10.2210/pdb6fmt/pdb
分子名称Undecaprenyl-diphosphatase, MERCURY (II) ION, (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate, ... (5 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., membrane protein, hydrolase
由来する生物種Escherichia coli K-12
タンパク質・核酸の鎖数1
化学式量合計32636.77
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: 2018-09-05, 最終更新日: 2024-06-19)
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
Cited by
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
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (3 Å)
構造検証レポート
Validation report summary of 6fmt
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-01-28に公開中

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