Expression, purification, and crystallization of meso-diaminopimelate dehydrogenase from Corynebacterium glutamicum

Sreelatha G. Reddy, Giovanna Scapin, John S. Blanchard

Research output: Contribution to journalArticle

14 Citations (Scopus)

Abstract

The gene encoding the meso-diaminopimelate dehydrogenase (DAPDH) from Corynebacterium glutamicum was overexpressed and purified to homogeneity. Crystals of the binary DAPDH-NADP+ complex were obtained from solutions of polyethylene glycol 8000, 100 mM sodium cacodylate, pH 6.5, and 150-300 mM Mg(OAc)2. The crystals diffract to 2.2 Å, belong to the orthorhombic space group P21, and contain two molecules per asymmetric unit.

Original languageEnglish (US)
Pages (from-to)514-516
Number of pages3
JournalProteins: Structure, Function and Genetics
Volume25
Issue number4
DOIs
StatePublished - 1996

Fingerprint

diaminopimelate dehydrogenase
Corynebacterium glutamicum
Crystallization
Purification
Cacodylic Acid
Crystals
Gene encoding
NADP
Sodium
Molecules
Genes

Keywords

  • D-amino acid
  • X-ray crystallography

ASJC Scopus subject areas

  • Genetics
  • Structural Biology
  • Biochemistry

Cite this

Expression, purification, and crystallization of meso-diaminopimelate dehydrogenase from Corynebacterium glutamicum. / Reddy, Sreelatha G.; Scapin, Giovanna; Blanchard, John S.

In: Proteins: Structure, Function and Genetics, Vol. 25, No. 4, 1996, p. 514-516.

Research output: Contribution to journalArticle

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