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

Authors
Korndorfer, IP Salerno, J Jing, D Matthews, BW
Citation
Ip. Korndorfer et al., Crystallization and preliminary X-ray analysis of a bacteriophage T4 primase fragment, ACT CRYST D, 56, 2000, pp. 95-97
Citations number
14
Categorie Soggetti
Chemistry & Analysis
Journal title
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
ISSN journal
09074449 → ACNP
Volume
56
Year of publication
2000
Part
1
Pages
95 - 97
Database
ISI
SICI code
0907-4449(200001)56:<95:CAPXAO>2.0.ZU;2-5
Abstract
The primase from bacteriophage T4 is a single-stranded DNA-dependent RNA po lymerase that is one of the seven proteins that constitute the DNA-replicat ion machinery of bacteriophage T4. In an attempt to crystallize the protein , a number of variants were generated. One such construct, which includes t he C-terminal region (residues 196-340), gave four different crystal forms which diffract in the 3.5-6.0 Angstrom resolution range.