Crystallization and preliminary X-ray analysis of a bacteriophage T4 primase fragment.
Crystallization and preliminary X-ray analysis of a bacteriophage T4 primase fragment.
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噬菌体 T4 引物酶片段的结晶和初步 X 射线分析。
DOI：
10.1107/s0907444999014225
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发表时间：
2000
期刊：
影响因子：
--
通讯作者：
Matthews,BW
中科院分区：
文献类型：
--
作者：
Korndörfer,IP;Salerno,J;Jing,D;Matthews,BW
T4噬菌体的启动子酶是一种依赖于DNA的单链RNA聚合酶，是构成T4噬菌体DNA复制机制的七种蛋白质之一。为了使蛋白质结晶，产生了许多变体。其中一个这样的结构，包括C-末端区域(残基196-340)，给出了四种不同的晶型，它们在3.56.0 ä分辨率范围内衍射。
The primase from bacteriophage T4 is a single-stranded DNA-dependent RNA polymerase that is one of the seven proteins that constitute the DNA-replication machinery of bacteriophage T4. In an attempt to crystallize the protein, a number of variants were generated. One such construct, which includes the C-terminal region (residues 196–340), gave four different crystal forms which diffract in the 3.5–6.0 Å resolution range.