Crystallization of the Soluble Lytic Transglycosylase from Escherichia coli K12

Henriette J. Rozeboom, Bauke W. Dijkstra, Henk Engel, Wolfgang Keck

Research output: Contribution to journalComment/Letter to the editorAcademicpeer-review

7 Citations (Scopus)
186 Downloads (Pure)


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 Å resolution. Their space group is P212121 with cell dimensions a=81 Å, b=88 Å and c=135 Å. Assuming one monomer (Mr 70,362) per asymmetric unit, the solvent content of these crystals is 63%.
Original languageEnglish
Pages (from-to)557-559
Number of pages3
JournalJournal of Molecular Biology
Issue number4
Publication statusPublished - 20-Apr-1990

Cite this