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首页> 外文期刊>Crystallography reports >Preparation, crystallization, and preliminary X-ray diffraction study of mutant carboxypeptidase T containing the primary specificity pocket of carboxypeptidase B
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Preparation, crystallization, and preliminary X-ray diffraction study of mutant carboxypeptidase T containing the primary specificity pocket of carboxypeptidase B

机译:含有羧肽酶B一级特异性口袋的突变型羧肽酶T的制备,结晶和初步X射线衍射研究

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摘要

Recombinant G215S, A251G, T257A, D260G, T262D mutant carboxypeptidase T from Thermoactinomyces vulgaris containing mutations in the primary specificity pocket was prepared and crystallized. Single crystals with a size of up to 0.3 mm were grown and investigated by X-ray diffraction. Recombinant mutant carboxypeptidase T containing the primary specificity subsite compositionally identical to that of pancreatic carboxypeptidase B crystallizes in the same space group as the natural enzyme. The crystals belong to sp. gr. P6 _322; the unit-cell parameters are a = b = 157.867 ?, c = 104.304 ?, α = β = 90°, γ = 120°. X-ray diffraction data suitable for determining the three-dimensional structure at atomic resolution were collected from one crystal.
机译:制备了来自寻常嗜热放线菌的重组G215S,A251G,T257A,D260G,T262D突变羧肽酶T,该重组羧肽酶T的一级特异性口袋中含有突变并结晶。生长尺寸最大为0.3mm的单晶并通过X射线衍射研究。包含与胰腺羧肽酶B组成相同的主要特异性亚位点的重组突变体羧肽酶T,在与天然酶相同的空间群中结晶。晶体属于sp。 gr。 P6 _322;晶胞参数为:a = b =157.867Ω,c =104.304Ω,α=β= 90°,γ= 120°。从一个晶体中收集适合于以原子分辨率确定三维结构的X射线衍射数据。

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