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6FMS

IMISX-EP of Se-LspA

Summary for 6FMS
Entry DOI10.2210/pdb6fms/pdb
Related PRD IDPRD_002257
DescriptorLipoprotein signal peptidase, Globomycin, (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate, ... (4 entities in total)
Functional Keywordsserial crystallography, experimental phasing, in meso crystallization, in situ diffraction data collection, membrane protein structure, membrane protein, hydrolase
Biological sourcePseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
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Total number of polymer chains8
Total formula weight95690.74
Authors
Huang, C.-Y.,Olieric, V.,Howe, N.,Warshamanage, R.,Weinert, T.,Panepucci, E.,Vogeley, L.,Basu, S.,Diederichs, K.,Caffrey, M.,Wang, M. (deposition date: 2018-02-02, release date: 2018-08-29, Last modification date: 2024-11-06)
Primary citationHuang, 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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3 Å)
Structure validation

237735

数据于2025-06-18公开中

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