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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Purification, characterization and crystallization in two crystal forms of bovine cyclophilin 40.
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Purification, characterization and crystallization in two crystal forms of bovine cyclophilin 40.

机译：纯化、表征和结晶在两个晶体形式的牛还有40。

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摘要

The purification and crystallization of two different crystal forms of the two-domain protein bovine cyclophilin 40 is reported. Tetragonal crystals grown in methyl pentanediol belong to space group P4222 with unit-cell parameters a = 94.5, c = 118.3 A. Long thin needles grown from PEG belong to space group C2 with unit-cell parameters a = 125.71, b = 47.3, c = 74.6 A, beta = 93.90 degrees. The N-terminal 170 amino acids have significant homology with the well characterized human cyclophilin A. The C-terminal domain is largely made up of three copies of the tetratricopeptide repeat motif thought to be involved in mediating protein-protein interactions. Cyclophilins are frequently found as domains in larger multidomain proteins. To date, only X-ray structures of single-domain cyclophilins have been reported, and this work provides the first example of the purification and crystallization of a larger protein containing a cyclophilin domain.
机译：两个的提纯和结晶不同的晶体形式的两个域蛋白质牛还有40报道。晶体生长在甲基戊二醇属于空间群P4222晶胞参数=94.5, c = 118.3。属于空间群C2与单胞挂钩参数= 125.71,= 47.3 b, c = 74.6,β= 93.90度。有明显的同源性,好吗还有人类a c端特点域在很大程度上是由三个副本tetratricopeptide重复主题思想参与调节蛋白质交互。域更大的多畴的蛋白质。日期,只有x射线单极结构还有报道,这项工作提供净化的第一个例子和一个更大的蛋白质结晶还有包含域。

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