一种催化缺陷型半合成核糖核酸酶的晶体，与完全有活性的亲本酶的晶体同晶型。

Crystals of a catalytically defective, semisynthetic ribonuclease isomorphous with those of the fully active parent enzyme.

作者信息

Doscher M S, Martin P D, Edwards B F

出版信息

J Mol Biol. 1983 Jun 5;166(4):685-7. doi: 10.1016/s0022-2836(83)80293-9.

Abstract

The enzymically active, semisynthetic, non-covalent complex formed by residues 1 through 118 and residues 111 through 124 of bovine pancreatic ribonuclease A crystallizes at pH 5.2 from (NH4)2SO4/CsCl solution with space group P3(2)21 and unit cell dimensions a and b = 67.7 A, c = 65.1 A and gamma = 120 degrees. The catalytically defective enzyme that results from the replacement of phenylalanine 120 by leucine crystallizes isomorphously with the parent structure (a and b = 67.2 A, c = 64.7 A, gamma = 120 degrees).

摘要

由牛胰核糖核酸酶A的1至118位残基与111至124位残基形成的具有酶活性的半合成非共价复合物，在pH 5.2条件下从(NH4)2SO4/CsCl溶液中结晶，空间群为P3(2)21，晶胞参数a和b = 67.7 Å，c = 65.1 Å，γ = 120°。由亮氨酸取代苯丙氨酸120而产生的催化缺陷型酶与母体结构同晶型结晶（a和b = 67.2 Å，c = 64.7 Å，γ = 120°）。