Nakai T, Okada K, Kawaguchi S, Kato R, Kuramitsu S, Hirotsu K
Department of Chemistry, Faculty of Science, Osaka City University, Sugimoto, Sumiyoshi-ku, Osaka 558, Japan.
Acta Crystallogr D Biol Crystallogr. 1998 Sep 1;54(Pt 5):1032-4. doi: 10.1107/s090744499800434x.
Recombinant aspartate aminotransferase from an extremely thermophilic bacterium, Thermus thermophilus HB8, has been crystallized in two different crystal forms. The crystals of both forms are orthorhombic and belong to space group P212121 with cell dimensions a = 124.3, b = 113.6 and c = 61.6 A for form I and a = 197.3, b = 109.7 and c = 80.3 A for form II. The crystals of form I and II diffract to 2.1 and 2.5 A resolution, respectively, on a conventional laboratory rotating-anode source. Two heavy-atom derivatives have been identified for form I.
来自嗜热栖热菌HB8（Thermus thermophilus HB8）的重组天冬氨酸转氨酶已形成两种不同的晶体形式。两种形式的晶体均为正交晶系，属于空间群P212121，晶胞参数为：晶型I的a = 124.3 Å、b = 113.6 Å、c = 61.6 Å；晶型II的a = 197.3 Å、b = 109.7 Å、c = 80.3 Å。在传统实验室旋转阳极光源上，晶型I和II的晶体分别衍射至2.1 Å和2.5 Å分辨率。已鉴定出晶型I的两种重原子衍生物。
