New crystal form of cytosolic chicken aspartate aminotransferase suitable for high-resolution X-ray analysis.
Four new crystal forms of chicken cytosolic aspartate aminotransferase have been grown from polyethylene glycol solutions. Crystals of the unliganded enzyme and of enzyme liganded with maleate diffract to 1.8 A resolution. Both the free and maleate-liganded enzymes crystallize in space group P2(1)2(1)2(1), but display slightly different cell dimensions (a = 56.9 A, b = 126.9 A and c = 124.6 A versus a = 56.5 A, b = 126.1 A and c = 124.6 A). The influence of various divalent metal ions, dioxane and non-ionic detergent beta-octylglucoside on crystallization has been investigated. The best crystals of liganded enzyme were obtained in the presence of Mg2+ ions, and these crystals were used for data collection to 1.9 A resolution.
Malashkevich
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Institute of Molecular Biology, Academy of Sciences of the U.S.S.R., Moscow.
Sinitzina
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D000818:Animals; D001219:Aspartate Aminotransferases / Q000737:chemistry*; D002645:Chickens; D003460:Crystallization; D003600:Cytosol / Q000737:chemistry*; D014961:X-Ray Diffraction
D001219:Aspartate Aminotransferases