2END
CRYSTAL STRUCTURE OF A PYRIMIDINE DIMER SPECIFIC EXCISION REPAIR ENZYME FROM BACTERIOPHAGE T4: REFINEMENT AT 1.45 ANGSTROMS AND X-RAY ANALYSIS OF THE THREE ACTIVE SITE MUTANTS
Replaces: 1ENDExperimental procedure
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 41.310, 40.110, 37.590 |
| Unit cell angles | 90.00, 90.04, 90.00 |
Refinement procedure
| Resolution | 6.000 - 1.450 |
| R-factor | 0.161 |
| RMSD bond length | 0.021 |
| RMSD bond angle | 0.039 |
| Refinement software | PROLSQ |
Data quality characteristics
| Overall | |
| High resolution limit [Å] | 1.450 * |
| Rmerge | 0.048 * |
| Completeness [%] | 80.2 * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 10 (mg/ml) | |
| 2 | 1 | drop | 50 (mM) | ||
| 3 | 1 | drop | sodium cacodylate/HCl | 8 (mM) | |
| 4 | 1 | drop | PEG4000 | 5 (%(w/v)) | |
| 5 | 1 | reservoir | PEG | 15 (%) |
