Open AccessCrystallization and preliminary X‐ray analysis of the CRP–cAMP–DNA (full length) complex
Author(s) -
Huang Jing,
Liu Jing,
Tao Wenbing,
Yang Zhenxing,
Qiu Rui,
Yu Shaoning,
Ji Chaoneng
Publication year - 2013
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309113009925
Subject(s) - crystallization , dna , crystallography , x ray , materials science , x ray crystallography , chemistry , physics , optics , biochemistry , diffraction , organic chemistry
The Escherichia coli cyclic AMP receptor protein (CRP) is a well known transcription activator protein. In this study, CRP was overexpressed, purified and cocrystallized with cAMP and a 38 bp full‐length double‐stranded DNA fragment. The full‐length segment differed from the half‐site fragments used in previous crystallization experiments and is more similar to the environment in vivo . CRP–cAMP–DNA crystals were obtained and diffracted to 2.9 Å resolution. The crystals belonged to space group P 3 1 21, with unit‐cell parameters a = b = 76.03, c = 144.00 Å. The asymmetric unit was found to contain one protein molecule and half a 38 bp full‐length double‐stranded DNA fragment, with a Matthews coefficient of 2.62 Å 3 Da −1 and a solvent content of 53.14%.