Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

6FMX

IMISX-EP of W-PgpB

Summary for 6FMX
Entry DOI10.2210/pdb6fmx/pdb
DescriptorPhosphatidylglycerophosphatase B, (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate, TUNGSTATE(VI)ION, ... (4 entities in total)
Functional Keywordsserial crystallography, experimental phasing, in meso crystallization, in situ diffraction data collection, membrane protein structure., membrane protein, hydrolase
Biological sourceBacillus subtilis (strain 168)
Total number of polymer chains1
Total formula weight27186.37
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: 2018-09-05, Last modification date: 2024-05-08)
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 (1.79 Å)
Structure validation

242842

数据于2025-10-08公开中

PDB statisticsPDBj update infoContact PDBjnumon