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Structure of Escherichia coli malate dehydrogenase at 1.45 Å resolution
Zaitseva, Jelena Meneely, Kathleen M. Lamb, Audrey L.
Zaitseva, Jelena
Meneely, Kathleen M.
Lamb, Audrey L.
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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, [beta] = 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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This is the publisher's version. Copyright 2009 by the International Union of Crystallography. For full text visit http://dx.doi.org/10.1107/S1744309109032217.
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2009-09
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International Union of Crystallography
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Lamb_v65p866-869.pdf
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Zaitseva, Jelena, Kathleen M. Meneely, and Audrey Lee Lamb. "Structure of Escherichia Coli Malate Dehydrogenase at 1.45 Å Resolution." Acta Crystallographica Section F Structural Biology and Crystallization Communications 65.9 (2009): 866-69. Wiley Oline Library. Web. 24 Apr. 2015. http://dx.doi.org/10.1107/S1744309109032217.