title: Purification, crystallization and preliminary X-ray analysis of the lytic transglycosylase MltA from Escherichia coli.
abstract: The lytic transglycosylase MltA from Escherichia coli with its membrane anchor and signal sequence deleted has been purified to homogeneity by means of cation-exchange chromatography. The enzyme was crystallized using the hanging-drop vapour-diffusion method. The crystals belong to space group P3(1)21 or P3(2)21, with unit-cell parameters a = b = 103.70, c = 109.84 A and one molecule per asymmetric unit. Crystals diffract to 2.2 A resolution on a synchrotron-radiation source.
authors.affiliation: Laboratory of Biophysical Chemistry, University of Groningen, Nijenborgh 4, 9747 AG Groningen, The Netherlands.
authors.forename: Karin E
authors.initials: KE
authors.lastname: Van Straaten
authors.forename: Bauke W
authors.initials: BW
authors.lastname: Dijkstra
authors.forename: Andy Mark W H
authors.initials: AM
authors.lastname: Thunnissen
mesh_terms: D003001:Cloning, Molecular; D003460:Crystallization; D018360:Crystallography, X-Ray; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000235:genetics; D016695:Glycosyltransferases / Q000737:chemistry*; D009154:Mutation; D012995:Solubility
chemical_list: D029968:Escherichia coli Proteins; D016695:Glycosyltransferases; C085441:MltA protein, bacteria