6FMR

IMISX-EP of Se-PepTSt

Summary for 6FMR

• Entry DOI: 10.2210/pdb6fmr/pdb
• Descriptor: Di-or tripeptide:H+ symporter, (2S)-2,3-DIHYDROXYPROPYL(7Z)-PENTADEC-7-ENOATE, PHOSPHATE ION, ... (4 entities in total)
• Functional Keywords: serial crystallography, experimental phasing, in meso crystallization, in situ diffraction data collection, membrane protein structure., transport protein
• Biological source: Streptococcus thermophilus (strain ATCC BAA-250 / LMG 18311)
• Total number of polymer chains: 1
• Total formula weight: 58136.28

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: 2018-10-10)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.7 Å)