title: Crystallization and preliminary x-ray diffraction analysis of malic enzyme from pigeon liver.
abstract: 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.
authors.affiliation: Institute of Molecular Biology, Academia Sinica, Taipei, Taiwan.
authors.forename: L C
authors.initials: LC
authors.lastname: Tsai
authors.forename: C C
authors.initials: CC
authors.lastname: Kuo
authors.forename: W Y
authors.initials: WY
authors.lastname: Chou
authors.forename: G G
authors.initials: GG
authors.lastname: Chang
authors.forename: H S
authors.initials: HS
authors.lastname: Yuan
mesh_terms: 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
chemical_list: D011994:Recombinant Proteins; D008291:Malate Dehydrogenase; C031917:malate dehydrogenase (oxaloacetate-decarboxylating) (NADP+)