1QHG
STRUCTURE OF DNA HELICASE MUTANT WITH ADPNP
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SRS |
| Synchrotron site | SRS |
| Temperature [K] | 287 |
| Detector technology | IMAGE PLATE |
| Detector | MARRESEARCH |
| Spacegroup name | P 65 |
| Unit cell lengths | 138.098, 138.098, 111.086 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 10.000 - 2.500 |
| R-factor | 0.22 |
| Rwork | 0.220 |
| R-free | 0.26900 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.015 |
| RMSD bond angle | 3.350 |
| Refinement software | X-PLOR |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 10.000 |
| High resolution limit [Å] | 2.500 |
| Rmerge | 0.610 |
| Number of reflections | 37521 |
| Completeness [%] | 92.3 |
| Redundancy | 2.36 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 7.5 * | 20 * | Bird, L.E., (1998) Nucl. Acids Res., 26, 2686. * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 10 (mg/ml) | |
| 2 | 1 | drop | Tris | 50 (mM) | |
| 3 | 1 | drop | 300 (mM) | ||
| 4 | 1 | reservoir | MES | 100 (mM) | |
| 5 | 1 | reservoir | sodium acetate | 1.0 (M) |
