Open AccessCrystallization and preliminary X‐ray analysis of phage Mu activator protein C in a complex with promoter DNA
Author(s) -
Shanmuganatham Karthik K.,
Ravichandran Manimekalai,
Howe Martha M.,
Park HeeWon
Publication year - 2007
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309107025286
Subject(s) - crystallization , dna , x ray , activator (genetics) , crystallography , microbiology and biotechnology , materials science , chemistry , biology , physics , genetics , gene , optics , organic chemistry
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 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 P 4 1 or P 4 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.