View source for 6fmw


==IMISX-EP of Hg-BacA cocrystallization==
<StructureSection load='6fmw' size='340' side='right'caption='[[6fmw]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6fmw]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6FMW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6FMW FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene>, <scene name='pdbligand=OLC:(2R)-2,3-DIHYDROXYPROPYL+(9Z)-OCTADEC-9-ENOATE'>OLC</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6fmw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fmw OCA], [https://pdbe.org/6fmw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6fmw RCSB], [https://www.ebi.ac.uk/pdbsum/6fmw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6fmw ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/UPPP_ECOLI UPPP_ECOLI] Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin.<ref>PMID:15778224</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.

In situ serial crystallography for rapid de novo membrane protein structure determination.,Huang CY, Olieric V, Howe N, Warshamanage R, Weinert T, Panepucci E, Vogeley L, Basu S, Diederichs K, Caffrey M, Wang M Commun Biol. 2018 Aug 27;1:124. doi: 10.1038/s42003-018-0123-6. eCollection 2018. PMID:30272004<ref>PMID:30272004</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6fmw" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli K-12]]
[[Category: Large Structures]]
[[Category: Basu S]]
[[Category: Caffrey M]]
[[Category: Diederichs K]]
[[Category: Howe N]]
[[Category: Huang C-Y]]
[[Category: Olieric V]]
[[Category: Panepucci E]]
[[Category: Vogeley L]]
[[Category: Wang M]]
[[Category: Warshamanage R]]
[[Category: Weinert T]]