PMID:15583400

Citation	Ma, C and Chang, G (2004) Crystallography of the integral membrane protein EmrE from Escherichia coli. Acta Crystallogr. D Biol. Crystallogr. 60:2399-402
Abstract	Crystals of the EmrE membrane-protein imposed several technical challenges for X-ray crystallography, including high mosaicity, poor diffraction and a relatively large number of heavy atoms. Consequently, the heavy-atom substructure solution was difficult to obtain. By removing the histidine tag for protein purification, the mosaicity and the diffraction quality were greatly improved. The direct-methods Shake-and-Bake program SnB was successful in locating the heavy-atom sites from a mutant of EmrE which lacks a cysteine and therefore has a reduction in the number of heavy-atom sites. The substructure solution was solved from data with anomalous difference at a resolution of 5.5 A and the structure was determined to 3.8 A.
Links	PubMed Online version:10.1107/S090744490402548X
Keywords	Antiporters/chemistry; Crystallography, X-Ray; Cysteine/chemistry; Drug Resistance, Multiple; Escherichia coli/metabolism; Escherichia coli Proteins; Histidine/chemistry; Membrane Proteins/chemistry; Models, Molecular; Mutation; Polymerase Chain Reaction; Protein Conformation
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