title: Preliminary crystallographic studies of human mitochondrial NAD(P)(+)-dependent malic enzyme.
abstract: Human mitochondrial NAD(P)(+)-dependent malic enzyme was overexpressed in Escherichia coli and purified by anion-exchange, ATP affinity, and gel filtration chromatography. The protein was crystallized with the hanging-drop vapor diffusion method. Many different crystal forms were observed, five of which were characterized in some detail. A 2.5-A multiple-wavelength anomalous diffraction data set and a 2.1-A native data set were collected using synchrotron radiation on crystals containing selenomethionyl residues. These crystals belong to space group B2, with a = 204.4 A, b = 107.0 A, c = 59.2 A, and gamma = 101.9 degrees. Self-rotation functions demonstrated that the tetramer of this enzyme obeys 222 symmetry.
authors.affiliation: Department of Biological Sciences, Columbia University, New York, New York, 10027, USA.
authors.forename: G
authors.initials: G
authors.lastname: Bhargava
authors.forename: S
authors.initials: S
authors.lastname: Mui
authors.forename: S
authors.initials: S
authors.lastname: Pav
authors.forename: H
authors.initials: H
authors.lastname: Wu
authors.forename: G
authors.initials: G
authors.lastname: Loeber
authors.forename: L
authors.initials: L
authors.lastname: Tong
mesh_terms: D003460:Crystallization; D018360:Crystallography, X-Ray; D006801:Humans; D008291:Malate Dehydrogenase / Q000737:chemistry* / Q000648:ultrastructure; D008928:Mitochondria / Q000737:chemistry* / Q000201:enzymology*; D012645:Selenomethionine / Q000737:chemistry
chemical_list: D012645:Selenomethionine; D008291:Malate Dehydrogenase; C031917:malate dehydrogenase (oxaloacetate-decarboxylating) (NADP+)