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Updated: Jun 13, 2026
Crystallization of Membrane Proteins in Lipidic Mesophases
Published on: March 28, 2011
Crystallization and preliminary X-ray analysis of the ligand-binding domain of cAMP receptor protein
Wenbing Tao1, Feng Li, Haiping Liu
1Department of Chemistry and Institute of Biomedical Science, Fudan University, Shanghai 200433, People's Republic of China.
Abstract:
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 A resolution and belonged to space group P2(1), with unit-cell parameters a = 59.7, b = 75.1, c = 128.3 A, beta = 91.5 degrees . Crystals of CH-CRP diffracted to 2.8 A resolution and belonged to space group P222, with unit-cell parameters a = 45.8, b = 60.9, c = 205.6 A.
