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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Crystallization and preliminary X-ray crystallographic studies of salt-tolerant glutaminase from Micrococcus luteus K-3.
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Crystallization and preliminary X-ray crystallographic studies of salt-tolerant glutaminase from Micrococcus luteus K-3.

机译：结晶和初步的x射线晶体的研究耐盐谷氨酰胺酶从微球菌危害k3。

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摘要

Glutaminase from the marine bacterium Micrococcus luteus K-3 (Micrococcus glutaminase) is a salt-tolerant protein which shows equivalent activities both in the absence and the presence of 3 M sodium chloride and is distinct from halophilic proteins, which are inactivated in the absence of salt. To investigate the mechanisms of the salt-tolerant adaptation of Micrococcus glutaminase, the glutaminase and its major fragment containing about 80% of the protein were crystallized using the hanging-drop vapour-diffusion method. The glutaminase crystals belong to space group P622, with unit-cell parameters a = b = 111.4, c = 210.9 A, alpha = beta = 90, gamma = 120 degrees, and diffract to 2.6 A resolution. The fragment crystals belong to space group F222, with unit-cell parameters a = 115.7, b = 116.4, c = 144.9 A, alpha = beta = gamma = 90 degrees, and diffract to 2.4 A resolution. Data from selenomethionine (SeMet) substituted glutaminase crystals and from SeMet-substituted fragment crystals were collected to 2.6 and 2.4 A resolution, respectively. Structural analyses of the glutaminase and its fragment are currently being attempted using the multiwavelength anomalous diffraction (MAD) phasing method.
机译：谷氨酰胺酶从海洋细菌微球菌是一种危害k3(微球菌谷氨酰胺酶)耐盐蛋白质显示等价的活动在没有和存在3 M氯化钠,截然不同嗜盐的蛋白质,这是灭活的没有盐。微球菌的耐盐适应谷氨酰胺酶、谷氨酰胺酶及其重要片段包含大约80%的蛋白质使用悬滴结晶vapour-diffusion方法。属于空间群P622,晶胞参数a = b = 111.4, c = 210.9,α=β= 90,γ= 120度,和衍射2.6一项决议。空间群F222,晶胞参数=115.7, b = 116.4, c = 144.9,α=β=γ= 90度,2.4和衍射决议。谷氨酰胺酶晶体和代替SeMet-substituted片段晶体是收集2.6和2.4一项决议,分别。谷氨酰胺酶及其片段正在试图用多波长反常衍射(疯狂)分阶段方法。

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