Crystallization and preliminary X-ray analysis of phage Mu activator protein C in a complex with promoter DNA
- Department of Molecular Sciences, University of Tennessee Health Science Center, Memphis, TN 38163 (United States)
- Structural Genomics Consortium, Department of Pharmacology, University of Toronto, Toronto, ON, M5G 1L5 (Canada)
The isolation and preliminary X-ray analysis of crystals of phage Mu activator protein C bound to promoter DNA are reported. Bacteriophage Mu C protein is an activator of the four Mu late promoters that drive the expression of genes encoding DNA-modification as well as phage head and tail morphogenesis proteins. This report describes the purification and cocrystallization of wild-type and selenomethionine-substituted C protein with a synthetic late promoter P{sub sym}, together with preliminary X-ray diffraction data analysis using SAD phasing. The selenomethionine peak data set was collected from a single crystal which diffracted to 3.1 Å resolution and belonged to space group P4{sub 1} or P4{sub 3}, with unit-cell parameters a = 68.9, c = 187.6 Å and two complexes per asymmetric unit. The structure will reveal the amino acid–DNA interactions and any conformational changes associated with DNA binding.
- OSTI ID:
- 22360355
- Journal Information:
- Acta Crystallographica. Section F, Vol. 63, Issue Pt 7; Other Information: PMCID: PMC2335125; PMID: 17620727; PUBLISHER-ID: en5234; OAI: oai:pubmedcentral.nih.gov:2335125; Copyright (c) International Union of Crystallography 2007; Country of input: International Atomic Energy Agency (IAEA); ISSN 1744-3091
- Country of Publication:
- United Kingdom
- Language:
- English
Similar Records
Crystallization and preliminary X-ray analysis of gene product 44 from bacteriophage Mu
Crystallization and preliminary crystallographic analysis of a family 43 β-d-xylosidase from Geobacillus stearothermophilus T-6