Abstract
Ocr, the product of gene 0.3 of bacteriophage T7, prevents the action of restriction endonucleases of the host bacteria. The amino-acid sequence of ocr has less than 20% similarity to any protein of known three-dimensional structure. Ocr has been crystallized in a number of different crystal forms and X-ray data for the seleno-L-methionine-substituted form has been collected to a resolution of 1.8 Angstrom. The presence of caesium was found to be required for good crystal growth. Anomalous X-ray data was used to identify possible positions for Se and Cs atoms in the unit cell.
| Original language | English |
|---|---|
| Pages (from-to) | 1652-1654 |
| Number of pages | 3 |
| Journal | Acta Crystallographica Section D: Biological Crystallography |
| Volume | 57 |
| Issue number | Part 11 |
| DOIs | |
| Publication status | Published - Nov 2001 |
Keywords / Materials (for Non-textual outputs)
- ocr
- gene 0.3
- bacteriophage
- anti-restriction