4.0 Article

Crystallization and preliminary X-ray analysis of a d-alanyl-d-alanine ligase (EcDdlB) from Escherichia coli

Publisher

INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S1744309110003970

Keywords

peptidoglycans; d-alanyl-d-alanine ligase; DdlB

Funding

  1. MRC [G500643, G0600801]
  2. Wellcome Trust [071998, 068598]
  3. MRC [G0500643, G0600801] Funding Source: UKRI
  4. Medical Research Council [G0600801, G0500643] Funding Source: researchfish

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A recombinant form of Escherichia coli DdlB (EcDdlB) has been prepared and cocrystallized with ADP and d-alanyl-d-alanine to represent the ternary complex of EcDdlB. Furthermore, EcDdlB has been cocrystallized under the same conditions with the ligands ATP and d-alanyl-d-alanine, representing the product-inhibited complex. The crystals belonged to space group P2(1)2(1)2(1), with unit-cell parameters a = 53.0, b = 97.6, c = 109.5 A and a = 51.2, b = 97.8, c = 110.1 A, respectively, and both contained two molecules in the asymmetric unit. Complete data sets were collected to 1.5 and 1.4 A resolution, respectively, from single crystals under cryogenic conditions using synchrotron radiation.

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