1HZ9
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 | 1999-05-01 |
Detector | MARRESEARCH |
Wavelength(s) | 1.5418 |
Spacegroup name | I 41 |
Unit cell lengths | 77.445, 77.445, 46.771 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 28.000 - 1.800 |
R-factor | 0.185 * |
Rwork | 0.185 |
R-free | 0.23400 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1c9o |
RMSD bond length | 0.011 |
RMSD bond angle | 2.500 |
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 | 1.830 |
High resolution limit [Å] | 1.800 | 1.800 |
Rmerge | 0.035 | 0.297 * |
Number of reflections | 12265 | |
<I/σ(I)> | 17.9 | 1.1 |
Completeness [%] | 94.7 | 68.3 * |
Redundancy | 3.1 * | 1.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7 * | 4 * | MPD, Na-Hepes, pH 7.5, 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 | MPD | 62 (%) | |
4 | 1 | reservoir | sodium HEPES | 100 (mM) |