Crystallization of the soluble lytic transglycosylase from Escherichia coli K12.
Lytic transglycosylases degrade the murein polymer of the bacterial cell wall to 1,6-anhydromuropeptides. These enzymes are of significant medical interest, not only because they are ideal targets for the development of new classes of antibiotics, but also because the low molecular weight products of their catalytic action can cause diverse biological activities in humans, which can be either beneficial or toxic. A soluble lytic transglycosylase was purified from an overproducing Escherichia coli strain and X-ray quality crystals were obtained at room temperature from hanging drops by vapor diffusion against 20 to 25% (NH4)2SO4, in 100 mM-sodium acetate buffer, pH 5.0. The crystals diffract in the X-ray beam to 2.8 A resolution. Their space group is P2(1)2(1)2(1) with cell dimensions a = 81 A, b = 88 A and c = 135 A. Assuming one monomer (Mr 70,362) per asymmetric unit, the solvent content of these crystals is 63%.
Rozeboom
H J
HJ
Department of Chemical Physics, University of Groningen, The Netherlands.
Dijkstra
B W
BW
Engel
H
H
Keck
W
W
D004926:Escherichia coli / Q000201:enzymology*; D016695:Glycosyltransferases; D015394:Molecular Structure; D012995:Solubility; D014166:Transferases; D014961:X-Ray Diffraction
D014166:Transferases; D016695:Glycosyltransferases; C021815:murein transglycosylase