Crystallization and preliminary X-ray analysis of a bacteriophage T4 primase fragment

Ingo P. Korndorfer; Jeffrey Salerno; Debra JingBrian W. Matthews

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Crystallization and preliminary X-ray analysis of a bacteriophage T4 primase fragment

机译：结晶和初步的x射线分析T4噬菌体引发酶片段

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The primase from bacteriophage T4 is a single-stranded DNA-dependent RNA polymerase that is one if the seven proteins that constitute the DNA-replication machinery of bacteriophage T4. In an attept 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 A resolution range.

机译：从T4噬菌体是一种引发酶单链RNA聚合酶如果七个蛋白质组成是T4噬菌体的dna复制机器。一个attept结晶蛋白质,许多变异生成。其中包括c端区域(残留196 - 340),给了四个不同的晶体形式衍射在3.5 - -6.0决议范围内。

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《Acta crystallographica.Section D. Biological crystallography》 |2000年第1期|95-97|共3页
作者
Ingo P. Korndorfer; Jeffrey Salerno; Debra JingBrian W. Matthews;
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作者单位

Institute of Molecular Biology, Howard Hughes Medical Institute and Department of Physics, 1229 University of Oregon, Eugene, Oregon 97403-1229, USA;

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原文格式 PDF
正文语种英语
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关键词
X-ray analysis; Bacteriophage T4; DNA PrimaseCrystallization;

机译：x射线分析;T4噬菌体;DNA;

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Crystallization and preliminary X-ray analysis of a bacteriophage T4 primase fragment

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