Crystallization of UDP-N-acetylglucosamine O-acyltransferase from Escherichia coli.
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 P2(1)3 (a = 99.0 A), diffract X-rays to approximately 2.5 A resolution and contain one subunit of the enzyme in the asymmetric unit.
Pfitzner
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Department of Biochemistry, Albert Einstein College of Medicine, Bronx, New York 10461, USA.
Raetz
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Roderick
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D000215:Acylation; D000217:Acyltransferases / Q000737:chemistry* / Q000302:isolation & purification; D004121:Dimethyl Sulfoxide / Q000737:chemistry; D004926:Escherichia coli / Q000201:enzymology; D015394:Molecular Structure; D010710:Phosphates / Q000737:chemistry; D011994:Recombinant Proteins / Q000737:chemistry; D014961:X-Ray Diffraction
D010710:Phosphates; D011994:Recombinant Proteins; D000217:Acyltransferases; C050304:acyl-(acyl-carrier-protein)-UDP-N-acetylglucosamine acyltransferase; D004121:Dimethyl Sulfoxide