1HZB
BACILLUS CALDOLYTICUS COLD-SHOCK PROTEIN MUTANTS TO STUDY DETERMINANTS OF PROTEIN STABILITY
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | EMBL/DESY, HAMBURG BEAMLINE BW7B |
| Synchrotron site | EMBL/DESY, HAMBURG |
| Beamline | BW7B |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2000-01-31 |
| Detector | MARRESEARCH |
| Wavelength(s) | 0.8428 |
| Spacegroup name | P 31 2 1 |
| Unit cell lengths | 51.579, 51.579, 101.149 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 8.000 - 1.280 |
| R-factor | 0.158 * |
| Rwork | 0.158 |
| R-free | 0.18900 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1C9O molecule A |
| RMSD bond length | 0.018 |
| RMSD bond angle | 2.700 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | EPMR |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 1.280 |
| High resolution limit [Å] | 1.270 | 1.270 |
| Rmerge | 0.024 | 0.185 * |
| Number of reflections | 40862 | |
| <I/σ(I)> | 41.4 | 1 |
| Completeness [%] | 97.5 | 94.7 |
| Redundancy | 3.5 | 2.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7 * | 20 * | MPD, cacodylate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 10-15 (mg/ml) | |
| 2 | 1 | drop | sodium-HEPES | 10 (mM) | |
| 3 | 1 | reservoir | MPD | 56 (%) | |
| 4 | 1 | reservoir | cacodylate | 100 (mM) |
