PMID:10666581
| Citation |
Yan, Y, Munshi, S, Li, Y, Pryor, KA, Marsilio, F and Leiting, B (1999) Crystallization and preliminary X-ray analysis of the Escherichia coli UDP-MurNAc-tripeptide D-alanyl-D-alanine-adding enzyme (MurF). Acta Crystallogr. D Biol. Crystallogr. 55:2033-4 |
|---|---|
| Abstract |
Crystals of the Escherichia coli UDP-MurNAc-tripeptide D-Ala-D-Ala-adding protein (MurF), which catalyzes the formation of the last metabolite of the bacterial cell-wall building block, have been grown in hanging-drop vapor-diffusion trials using PEG 8K as a precipitating agent. The crystals belong to hexagonal space group P6(1) or P6(5), with unit-cell dimensions a = b = 74, c = 425 A. The asymmetric unit contains two molecules, with a crystal volume per protein mass (V(m)) of 3.4 A(3) Da(-1) and a solvent content of about 64% by volume. A native data set to 2.8 A resolution has been obtained from a frozen crystal using a synchrotron X-ray source. |
| Links | |
| Keywords |
Base Sequence; Crystallization; Crystallography, X-Ray; DNA Primers/genetics; Escherichia coli/enzymology; Escherichia coli/genetics; Gene Expression; Peptide Synthases/chemistry; Peptide Synthases/genetics; Peptide Synthases/isolation & purification; Recombinant Proteins/chemistry; Recombinant Proteins/genetics; Recombinant Proteins/isolation & purification |
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