title: Preliminary X-ray crystallographic study of malate dehydrogenases from the thermoacidophilic Archaebacteria Thermoplasma acidophilum and Sulfolobus acidocaldarius.
abstract: Malate dehydrogenases from the thermoacidophilic Archaebacteria Thermoplasma acidophilum and Sulfolobus acidocaldarius have been crystallized and characterized by X-ray diffraction measurements. Crystals of the enzyme from T. acidophilum display space-group symmetry P2(1), a = 63 A, b = 135 A, c = 83 A and beta = 105 degrees; they scattered to approximately 4 A resolution. Two crystal modifications of malate dehydrogenase from S. acidocaldarius were characterized; one displayed trigonal symmetry corresponding to space groups P321, P3(1)21 or P3(2)21 with lattice parameters a = 151 A and c = 248 A and with resolution approximately to 5 A, whereas the other modification displayed space group symmetry I23 or I2(1)3 with lattice parameters a = 129 A and approximately 4.5 A resolution.
authors.affiliation: Institut für Organische Chemie, Biochemie und Isotopenforschung der Universität Stuttgart, F.R.G.
authors.forename: J J
authors.initials: JJ
authors.lastname: Stezowski
authors.forename: R
authors.initials: R
authors.lastname: Englmaier
authors.forename: C
authors.initials: C
authors.lastname: Galdiga
authors.forename: T
authors.initials: T
authors.lastname: Hartl
authors.forename: I
authors.initials: I
authors.lastname: Rommel
authors.forename: Z
authors.initials: Z
authors.lastname: Dauter
authors.forename: H
authors.initials: H
authors.lastname: Görisch
authors.forename: W
authors.initials: W
authors.lastname: Grossebüter
authors.forename: K
authors.initials: K
authors.lastname: Wilson
authors.forename: D
authors.initials: D
authors.lastname: Musil
mesh_terms: D001105:Archaea / Q000201:enzymology*; D001419:Bacteria / Q000201:enzymology*; D008291:Malate Dehydrogenase; D014961:X-Ray Diffraction
chemical_list: D008291:Malate Dehydrogenase