1HZA
BACILLUS CALDOLYTICUS COLD-SHOCK PROTEIN MUTANTS TO STUDY DETERMINANTS OF PROTEIN STABILITY
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU RU200 |
| Temperature [K] | 110 |
| Detector technology | IMAGE PLATE |
| Collection date | 1999-06-06 |
| Detector | MARRESEARCH |
| Wavelength(s) | 1.5418 |
| Spacegroup name | I 41 |
| Unit cell lengths | 76.418, 76.418, 47.463 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 28.000 - 1.800 |
| R-factor | 0.193 * |
| Rwork | 0.193 |
| R-free | 0.24600 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1c9o |
| RMSD bond length | 0.010 |
| RMSD bond angle | 2.700 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 28.000 | 1.820 |
| High resolution limit [Å] | 1.800 | 1.800 |
| Rmerge | 0.051 | 0.339 |
| Number of reflections | 9838 | |
| <I/σ(I)> | 19.1 | 1.3 |
| Completeness [%] | 75.9 | 39.6 |
| Redundancy | 2.1 | 1.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7 * | 20 * | PEG 800, sodium chloride, cacodylate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K |
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 | PEG8000 | 20 (%) | |
| 4 | 1 | reservoir | cacodylate | 100 (mM) | |
| 5 | 1 | reservoir | 200 (mM) |
