1ENK
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
Experimental procedure
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 41.700, 40.200, 37.100 |
| Unit cell angles | 90.00, 92.00, 90.00 |
Refinement procedure
| Resolution | 10.000 - 2.000 |
| R-factor | 0.207 |
| RMSD bond length | 0.016 |
| RMSD bond angle | 0.040 |
| Refinement software | PROLSQ |
Data quality characteristics
| Overall | |
| High resolution limit [Å] | 2.000 * |
| Rmerge | 0.084 * |
| Completeness [%] | 93.0 * |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion * | 7.5 * | 4 * | Morikawa, K., (1988) J. Mol. Biol., 202, 683. * |
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 (%) |
