Crystallization of UDP‐ N ‐acetylglucosamine  O ‐acyltransferase from  Escherichia coli | Zendy

Pfitzner Ute | Zendy; Raetz Christian R. H | Zendy; Roderick Steven L. | Zendy

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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.

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