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Crystallization of the soluble lytic transglycosylase from Escherichia coli K12.
J Mol Biol. 1990 Apr 20; 212(4):557-9.JM

Abstract

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%.

Authors+Show Affiliations

Rozeboom HJ
Department of Chemical Physics, University of Groningen, The Netherlands.
Dijkstra BW
No affiliation info available
Engel H
No affiliation info available
Keck W
No affiliation info available

MeSH

Escherichia coliGlycosyltransferasesMolecular StructureSolubilityTransferasesX-Ray Diffraction

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

2184239

Citation

Rozeboom, H J., et al. "Crystallization of the Soluble Lytic Transglycosylase From Escherichia Coli K12." Journal of Molecular Biology, vol. 212, no. 4, 1990, pp. 557-9.
Rozeboom HJ, Dijkstra BW, Engel H, et al. Crystallization of the soluble lytic transglycosylase from Escherichia coli K12. J Mol Biol. 1990;212(4):557-9.
Rozeboom, H. J., Dijkstra, B. W., Engel, H., & Keck, W. (1990). Crystallization of the soluble lytic transglycosylase from Escherichia coli K12. Journal of Molecular Biology, 212(4), 557-9.
Rozeboom HJ, et al. Crystallization of the Soluble Lytic Transglycosylase From Escherichia Coli K12. J Mol Biol. 1990 Apr 20;212(4):557-9. PubMed PMID: 2184239.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Crystallization of the soluble lytic transglycosylase from Escherichia coli K12. AU - Rozeboom,H J, AU - Dijkstra,B W, AU - Engel,H, AU - Keck,W, PY - 1990/4/20/pubmed PY - 1990/4/20/medline PY - 1990/4/20/entrez SP - 557 EP - 9 JF - Journal of molecular biology JO - J Mol Biol VL - 212 IS - 4 N2 - 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%. SN - 0022-2836 UR - https://www.unboundmedicine.com/medline/citation/2184239/Crystallization_of_the_soluble_lytic_transglycosylase_from_Escherichia_coli_K12_ DB - PRIME DP - Unbound Medicine ER -