Preliminary X-ray diffraction analysis of a crystallizable mutant of malate dehydrogenase from the thermophile Thermus flavus.
Malate dehydrogenase from mutant strain F428 of the thermophilic bacterium Thermus flavus has now been crystallized from polyethylene glycol 8000 in a form suitable for diffraction studies. The protein crystallizes in the orthorhombic P2(1)2(1)2(1) space group with unit cell dimensions a = 71.8 A, b = 88.6 A, c = 119.0 A. The asymmetric unit consists of one homodimer of molecular mass 67,000 Da. The X-ray diffraction extends beyond 1.7 A and a full data set to 1.9 A has been collected.
Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St Louis, MO 63110.
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Kelly
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Sarfaty
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Nishiyama
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Beppu
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Birktoft
D003460:Crystallization; D008291:Malate Dehydrogenase / Q000737:chemistry / Q000235:genetics*; D016296:Mutagenesis; D011487:Protein Conformation; D013824:Thermus / Q000201:enzymology / Q000235:genetics*; D014961:X-Ray Diffraction
D008291:Malate Dehydrogenase