Structure of Escherichia coli malate dehydrogenase at 1.45 Å resolution
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 BALB...
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Veröffentlicht in: | Acta crystallographica. Section F, Structural biology and crystallization communications Structural biology and crystallization communications, 2009-09, Vol.65 (9), p.866-869 |
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Hauptverfasser: | , , |
Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | 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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ISSN: | 1744-3091 1744-3091 |
DOI: | 10.1107/S1744309109032217 |