Open AccessCrystallization and preliminary X‐ray analysis of the ligand‐binding domain of cAMP receptor protein
Author(s) -
Tao Wenbing,
Li Feng,
Liu Haiping,
Bao Xiangyu,
Gong Weimin,
Yu Shaoning
Publication year - 2010
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309110008675
Subject(s) - subtilisin , resolution (logic) , crystallization , chymotrypsin , escherichia coli , chemistry , crystallography , ligand (biochemistry) , receptor , trypsin , microbiology and biotechnology , gene , biochemistry , biology , enzyme , organic chemistry , artificial intelligence , computer science
The cyclic AMP receptor protein (CRP) from Escherichia coli regulates the expression of a large number of genes. In this work, CRP has been overexpressed, purified and digested by subtilisin and chymotrypsin. The fragments S‐CRP (digested by subtilisin) and CH‐CRP (digested by chymotrypsin) have been purified and crystallized. Crystals of S‐CRP diffracted to 2.0 Å resolution and belonged to space group P 2 1 , with unit‐cell parameters a = 59.7, b = 75.1, c = 128.3 Å, β = 91.5°. Crystals of CH‐CRP diffracted to 2.8 Å resolution and belonged to space group P 222, with unit‐cell parameters a = 45.8, b = 60.9, c = 205.6 Å.