Preliminary X-ray crystallographic study of malate dehydrogenases from the thermoacidophilic Archaebacteria Thermoplasma acidophilum and Sulfolobus acidocaldarius.
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.
Stezowski
J J
JJ
Institut für Organische Chemie, Biochemie und Isotopenforschung der Universität Stuttgart, F.R.G.
Englmaier
R
R
Galdiga
C
C
Hartl
T
T
Rommel
I
I
Dauter
Z
Z
Görisch
H
H
Grossebüter
W
W
Wilson
K
K
Musil
D
D
D001105:Archaea / Q000201:enzymology*; D001419:Bacteria / Q000201:enzymology*; D008291:Malate Dehydrogenase; D014961:X-Ray Diffraction
D008291:Malate Dehydrogenase