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Crystallization of UDP‐ N ‐acetylglucosamine O ‐acyltransferase from Escherichia coli
Author(s) -
Pfitzner Ute,
Raetz Christian R. H,
Roderick Steven L.
Publication year - 1995
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.340220212
Subject(s) - escherichia coli , acyltransferase , crystallization , chemistry , potassium , resolution (logic) , crystallography , protein subunit , sodium , potassium phosphate , enzyme , biochemistry , stereochemistry , chromatography , organic chemistry , artificial intelligence , computer science , gene
Crystals of UDP‐ N ‐acetylglucosamine O ‐acyltransferase ( lpxA ) from Escherichia coli have been obtained from solutions of sodium/potassium phosphate and dimethylsulfoxide. These crystals belong to the cubic space group P 2 1 3 ( a = 99.0 Å), diffract X‐raysto approximately 2.5 Å resolution and contain one subunit of the enzyme in the asymmetric unit. © 1995 Wiley‐Liss, Inc.