title: Crystallization and preliminary X-ray analysis of the CRP-cAMP-DNA (full length) complex.
abstract: 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 P3121, 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%.
authors.affiliation: State Key Laboratory of Genetic Engineering, Institute of Genetics, School of Life Sciences, Fudan University, Shanghai 200433, PR China.
authors.forename: Jing
authors.initials: J
authors.lastname: Huang
authors.forename: Jing
authors.initials: J
authors.lastname: Liu
authors.forename: Wenbing
authors.initials: W
authors.lastname: Tao
authors.forename: Zhenxing
authors.initials: Z
authors.lastname: Yang
authors.forename: Rui
authors.initials: R
authors.lastname: Qiu
authors.forename: Shaoning
authors.initials: S
authors.lastname: Yu
authors.forename: Chaoneng
authors.initials: C
authors.lastname: Ji
mesh_terms: D003460:Crystallization; D018360:Crystallography, X-Ray; D002373:Cyclic AMP Receptor Protein / Q000032:analysis / Q000737:chemistry*; D004926:Escherichia coli; D029968:Escherichia coli Proteins / Q000737:chemistry*
chemical_list: D002373:Cyclic AMP Receptor Protein; D029968:Escherichia coli Proteins; C481662:crp protein, E coli
keywords: AMP receptor proteins; CRP; cAMP