Volume 65, Issue 9 pp. 866-869

Structure of Escherichia coli malate dehydrogenase at 1.45 Å resolution

Jelena Zaitseva

Jelena Zaitseva

Department of Molecular Biosciences, University of Kansas, Lawrence, Kansas 66045, USA

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Kathleen M. Meneely

Kathleen M. Meneely

Department of Molecular Biosciences, University of Kansas, Lawrence, Kansas 66045, USA

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Audrey L. Lamb

Audrey L. Lamb

Department of Molecular Biosciences, University of Kansas, Lawrence, Kansas 66045, USA

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First published: 21 September 2009
Audrey L. Lamb, e-mail: [email protected]

Abstract

The structure of apo malate dehydrogenase from Escherichia coli has been determined to 1.45 Å resolution. The crystals belonged to space group C2, with unit-cell parameters a = 146.0, b = 52.0, c = 168.9 Å, β = 102.2°. The structure was determined with the molecular-replacement pipeline program BALBES and was refined to a final R factor of 18.6% (Rfree = 21.4%). The final model has two dimers in the asymmetric unit. In each dimer one monomer contains the active-site loop in the open conformation, whereas in the opposing monomer the active-site loop is disordered.

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