Crystallization of a tryptic core of the single-stranded DNA binding protein of bacteriophage T4.
Crystallization of a tryptic core of the single-stranded DNA binding protein of bacteriophage T4.
复制标题
噬菌体 T4 的单链 DNA 结合蛋白的胰蛋白酶核心的结晶。
DOI：
10.1016/0022-2836(82)90321-7
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发表时间：
1982
影响因子：
5.6
通讯作者：
Williams,KR
中科院分区：
文献类型：
--
作者：
McKay,DB;Williams,KR
噬菌体T4的单链DNA结合蛋白或基因32蛋白的色氨酸核心（残基22至253）已结晶为四种不同的晶体形式。其中一种形式似乎适合于高分辨率x射线晶体学研究。三斜，空间群PI， a= 67.7 a°，b= 67.8 a°，c= 66.0 a°，α= 101.6°，β= 107.0°，γ= 105.2°。三种蛋白质原形成体在细胞内呈近菱形排列。
A tryptic core (residues 22 to 253) of the single-stranded DNA binding protein, or gene 32 protein, of bacteriophage T4 has been crystallized in four different crystal forms. One of these forms appears suitable for high-resolution X-ray crystallographic studies. It is triclinic, space group PI, with a= 67.7 A ̊, b= 67.8 A ̊, c= 66.0 A ̊, α= 101.6°, β= 107.0°, γ= 105.2°. There appear to be three protein protomers in a near-rhombohedral packing in the unit cell.