title: Crystallization and preliminary X-ray analysis of a bacteriophage T4 primase fragment.
abstract: 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 A resolution range.
authors.affiliation: Institute of Molecular Biology, Howard Hughes Medical Institute and Department of Physics, 1229 University of Oregon, Eugene, Oregon 97403-1229, USA.
authors.forename: I P
authors.initials: IP
authors.lastname: Korndörfer
authors.forename: J
authors.initials: J
authors.lastname: Salerno
authors.forename: D
authors.initials: D
authors.lastname: Jing
authors.forename: B W
authors.initials: BW
authors.lastname: Matthews
mesh_terms: D000595:Amino Acid Sequence; D017122:Bacteriophage T4 / Q000201:enzymology* / Q000235:genetics; D003001:Cloning, Molecular; D003460:Crystallization; D018360:Crystallography, X-Ray; D019915:DNA Primase / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification*; D004926:Escherichia coli / Q000235:genetics; D015870:Gene Expression; D005814:Genes, Viral; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification*
chemical_list: D010446:Peptide Fragments; D019915:DNA Primase