title: Crystallization and preliminary X-ray analysis of the Escherichia coli UDP-MurNAc-tripeptide D-alanyl-D-alanine-adding enzyme (MurF).
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.
authors.affiliation: Department of Antiviral Research, Merck Research Laboratories, West Point, PA 19486, USA.
authors.forename: Y
authors.initials: Y
authors.lastname: Yan
authors.forename: S
authors.initials: S
authors.lastname: Munshi
authors.forename: Y
authors.initials: Y
authors.lastname: Li
authors.forename: K A
authors.initials: KA
authors.lastname: Pryor
authors.forename: F
authors.initials: F
authors.lastname: Marsilio
authors.forename: B
authors.initials: B
authors.lastname: Leiting
mesh_terms: D001483:Base Sequence; D003460:Crystallization; D018360:Crystallography, X-Ray; D017931:DNA Primers / Q000235:genetics; D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics; D015870:Gene Expression; D010453:Peptide Synthases / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification*; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification
chemical_list: D017931:DNA Primers; D011994:Recombinant Proteins; D010453:Peptide Synthases; C060628:UDP-N-acetylmuramoylalanyl-D-glutamyllysine-D-alanyl-D-alanine ligase