1WTV
Hyperthermophile chromosomal protein SAC7D single mutant M29A in complex with DNA GTAATTAC
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSRRC BEAMLINE BL17B2 |
| Synchrotron site | NSRRC |
| Beamline | BL17B2 |
| Temperature [K] | 150 |
| Detector technology | IMAGE PLATE |
| Collection date | 2002-11-29 |
| Detector | RIGAKU RAXIS IV++ |
| Wavelength(s) | 1.11634 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 35.923, 47.968, 77.777 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 30.000 - 1.600 |
| R-factor | 0.2132 |
| Rwork | 0.210 |
| R-free | 0.23800 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1azq |
| RMSD bond length | 0.017 |
| RMSD bond angle | 1.790 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | CNS |
| Refinement software | CNS |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 1.660 |
| High resolution limit [Å] | 1.600 | 1.600 |
| Rmerge | 0.049 | 0.490 |
| Number of reflections | 17958 | |
| <I/σ(I)> | 24 | 2.8 |
| Completeness [%] | 98.0 | 96.8 |
| Redundancy | 3.6 | 3.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7 | 298 | PEG 400, Tris buffer , pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 298.0K |
Crystallization Reagents
| ID | crystal ID | solution ID | reagent name | concentration | details |
| 1 | 1 | 1 | PEG 400 | ||
| 2 | 1 | 1 | Tris buffer | ||
| 3 | 1 | 2 | PEG 400 | ||
| 4 | 1 | 2 | Tris buffer |
