Crystallization and preliminary x-ray diffraction analysis of malic enzyme from pigeon liver.
Recombinant pigeon-liver malic enzyme was expressed in Escherichia coli and purified to homogeneity. Two different crystal forms were grown by the hanging-drop vapour-diffusion method. Both types of crystals belong to the tetragonal space group P4(2)22, with unit-cell dimensions a = b = 163.8, c = 174.3 A for the octahedral crystals and a = b = 124.5, c = 179.2 A for the rod-like crystals. X-ray diffraction data were collected at 100 K using a synchrotron-radiation X-ray source. The Matthews parameter suggests that there are four and two molecules per asymmetric unit for the larger and the smaller tetragonal unit cells, respectively.
Tsai
L C
LC
Institute of Molecular Biology, Academia Sinica, Taipei, Taiwan.
Kuo
C C
CC
Chou
W Y
WY
Chang
G G
GG
Yuan
H S
HS
D000818:Animals; D010856:Columbidae; D003460:Crystallization; D018360:Crystallography, X-Ray; D004926:Escherichia coli; D008099:Liver / Q000201:enzymology; D008291:Malate Dehydrogenase / Q000737:chemistry*; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry
D011994:Recombinant Proteins; D008291:Malate Dehydrogenase; C031917:malate dehydrogenase (oxaloacetate-decarboxylating) (NADP+)