1WTX
Hyperthermophile chromosomal protein SAC7D single mutant V26A in complex with DNA GTAATTAC
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU MICROMAX-002 |
Temperature [K] | 150 |
Detector technology | IMAGE PLATE |
Collection date | 2001-01-01 |
Detector | RIGAKU RAXIS IV |
Wavelength(s) | 1.5418 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 36.113, 50.443, 78.153 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 30.890 - 2.200 |
R-factor | 0.2253 |
Rwork | 0.224 |
R-free | 0.25300 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1azq |
RMSD bond length | 0.016 |
RMSD bond angle | 1.580 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | CNS |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.280 |
High resolution limit [Å] | 2.200 | 2.200 |
Rmerge | 0.042 | 0.403 |
Number of reflections | 7491 | |
<I/σ(I)> | 17 | 2.9 |
Completeness [%] | 97.1 | 88.7 |
Redundancy | 4.3 | 3.4 |
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 |