Expression, purification, and crystallization of meso-diaminopimelate dehydrogenase from Corynebacterium glutamicum.
The gene encoding the meso-diaminopimelate dehydrogenase (DAPDH) from Corynebacterium glutamicum was over-expressed 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 A, belong to the orthorhombic space group P2(1), and contain two molecules per asymmetric unit.
Reddy
S G
SG
Department of Biochemistry, Albert Einstein College of Medicine, Bronx, New York 10461, USA.
Scapin
G
G
Blanchard
J S
JS
D000594:Amino Acid Oxidoreductases / Q000737:chemistry / Q000235:genetics* / Q000302:isolation & purification; D003352:Corynebacterium / Q000201:enzymology*; D003460:Crystallization; D004591:Electrophoresis, Polyacrylamide Gel
D000594:Amino Acid Oxidoreductases; C020032:diaminopimelate dehydrogenase