Purification, crystallization and preliminary X-ray analysis of the lytic transglycosylase MltA from Escherichia coli.
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.
Van Straaten
Karin E
KE
Laboratory of Biophysical Chemistry, University of Groningen, Nijenborgh 4, 9747 AG Groningen, The Netherlands.
Dijkstra
Bauke W
BW
Thunnissen
Andy Mark W H
AM
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
D029968:Escherichia coli Proteins; D016695:Glycosyltransferases; C085441:MltA protein, bacteria