Article
Crystallization and preliminary X-ray diffraction analysis of D53H mutant Escherichia coli cAMP receptor protein.
Acta crystallographica. Section F, Structural biology and crystallization communications - 1 Dec 2013
Huang Jing, Wu Tong, Guo Zheng, Lou Tiantian, Yu Shaoning, Gong Weimin, Ji Chaoneng
Abstract excerpt
The Escherichia coli cyclic AMP receptor protein (CRP) is a prokaryotic global transcription activator protein that controls the expression of many different genes. Wild-type CRP can bind to special DNA sequences in the presence of cAMP. The substitution of Asp53 by His results in the CRP* phenotype, which does not require exogenous cAMP. In the present study, the D53H CRP mutant was overexpressed, purified and...
Topics
- Amino Acid Substitution
- Crystallization
- Crystallography, X-Ray
- Cyclic AMP
- Cyclic AMP Receptor Protein
- DNA, Bacterial
- Escherichia coli
- Gene Expression
- Mutation
- Protein Binding
- Protein Multimerization
- Recombinant Proteins