Crystallization of Escherichia coli enoyl reductase and its complex with diazaborine

Clair Baldock, John B. Rafferty, Svetlana E. Sedelnikova, Sian Bithell, Antoine R. Stuitje, Antoni R. Slabas, David W. Rice

    Research output: Contribution to journalArticlepeer-review


    Recent work has shown that the NADH-dependent enoyl acyl carrier protein reductase from Escherichia coli is the target for diazaborine, an antibacterial agent. This enzyme has been crystallized by the hanging-drop method of vapour diffusion complexed with NAD+ and in the presence and absence of a thieno diazaborine. The crystals grown in the absence of diazaborine (from A) are in the space group P21 with unit-cell dimensions a = 74.0, b = 81.2, c = 79.0 Å and β = 92.9°and with a tetramer in the asymmetric unit, whilst those grown in the presence of diazaborine (form B) are in the space group P6122 (or P6522) with unit-cell dimensions a = b = 80.9 and c = 328.3 Å, and with a dimer in the asymmetric unit. The structure will provide information on the nature of the drug binding site and contribute to a programme of rational drug design.
    Original languageEnglish
    Pages (from-to)1181-1184
    Number of pages3
    JournalActa Crystallographica Section D: Biological Crystallography
    Issue number6
    Publication statusPublished - 1996


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