Article
Expression, purification, and crystallization of natural and selenomethionyl recombinant ribonuclease H from Escherichia coli.
The Journal of biological chemistry - 15 Aug 1990
Yang W, Hendrickson W A, Kalman E T, Crouch R J
Abstract excerpt
Ribonuclease H (RNase H) from Escherichia coli is an endonuclease that specifically degrades the RNAs of RNA:DNA hybrids. The enzyme is a single polypeptide chain of 155 amino acid residues, of which 4 are methionines. To solve the crystallographic three-dimensional structure of E. coli RNase H b...
Topics
- Chromatography, DEAE-Cellulose
- Chromatography, High Pressure Liquid
- Chromatography, Ion Exchange
- Crystallization
- Enzyme Stability
- Escherichia coli
- Gene Expression
- Mutation
- Protein Conformation
- Recombinant Proteins
- Ribonucleases
- Selenium
- Selenomethionine
- Temperature
- X-Ray Diffraction