Purification and crystallization of recombinant Escherichia coli malate dehydrogenase

Michael D. Hall, David G. Levitt, Lee McAllister-Henn, Leonard J. Banaszak

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Malate dehydrogenase from Escherichia coli has been crystallized with polyethylene glycol and citrate buffer at pH 5·7. The enzyme was obtained from an E. coli strain in which the chromosomal malate dehydrogenase gene was contained on a pBR322 vector. Two types of crystals have been observed; a monoclinic C2 form and an orthorhombic C2221 form, which is found infrequently. Monoclinic crystals were used as seeds in several rounds of crystallization until large crystals suitable for diffraction analysis were available. A complete X-ray data set to 2·0 Å has been collected.

Original languageEnglish (US)
Pages (from-to)551-553
Number of pages3
JournalJournal of Molecular Biology
Issue number3
StatePublished - Aug 5 1991

Bibliographical note

Funding Information:
The eMDH project was supported by the National Science Foundation, U.S.A. (L.J.B., DNB 8941746) and the NTH (T,.M.-H., GM33218).


  • MDH
  • MDHase
  • citric acid cycle
  • dehydrogenase
  • malate dehydrogenase


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