1I5F
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 BW7A |
| Synchrotron site | EMBL/DESY, HAMBURG |
| Beamline | BW7A |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 1998-05-19 |
| Detector | MARRESEARCH |
| Wavelength(s) | 0.9493 |
| Spacegroup name | I 41 |
| Unit cell lengths | 77.120, 77.120, 48.260 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 15.000 - 1.400 |
| R-factor | 0.139 |
| Rwork | 0.139 |
| R-free | 0.20500 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1c9o |
| RMSD bond length | 0.007 * |
| RMSD bond angle | 0.023 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | SHELXL-97 |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 15.000 | 1.410 |
| High resolution limit [Å] | 1.400 | 1.400 |
| Rmerge | 0.044 * | 0.329 * |
| Number of reflections | 26715 | |
| <I/σ(I)> | 18.9 | 2.6 |
| Completeness [%] | 96.0 * | 92.6 * |
| Redundancy | 5.4 * |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7 * | 4 * | PEG 6000, sodium citrate, ammonia sulfate, pH 5.6, 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 | PEG6000 | 30 (%) | |
| 4 | 1 | reservoir | sodium citrate | 100 (mM) | |
| 5 | 1 | reservoir | ammonium sulfate | 200 (mM) |
