Crystallization and preliminary crystallographic studies of chloroplast NADP-dependent malate dehydrogenase from Flaveria bidentis.
Crystals of chloroplast NADP-dependent malate dehydrogenase have been grown both with and without the cofactor NADP present. The enzyme has a molecular weight of 43 kDa per subunit and exists as a dimer in solution. The crystals diffract to 2.8 A and belong to the space group P3221 with cell dimensions a = 148.1, c = 65.5 A.
MacPherson
K H
KH
Research School of Chemistry, Australian National University, GPO Box 414, Canberra, ACT 2601, Australia.
Ashton
A R
AR
Carr
P D
PD
Trevanion
S J
SJ
Verger
D
D
Ollis
D L
DL
D002736:Chloroplasts / Q000201:enzymology*; D003460:Crystallization; D018360:Crystallography, X-Ray; D008291:Malate Dehydrogenase / Q000737:chemistry*; D050538:Malate Dehydrogenase (NADP+); D010940:Plant Proteins / Q000737:chemistry*; D011487:Protein Conformation; D013696:Temperature
D010940:Plant Proteins; D008291:Malate Dehydrogenase; D050538:Malate Dehydrogenase (NADP+)