3A0J
Crystal structure of cold shock protein 1 from Thermus thermophilus HB8
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL44B2 |
| Synchrotron site | SPring-8 |
| Beamline | BL44B2 |
| Temperature [K] | 90 |
| Detector technology | CCD |
| Collection date | 2008-07-23 |
| Detector | ADSC QUANTUM 210 |
| Wavelength(s) | 1.00 |
| Spacegroup name | P 1 |
| Unit cell lengths | 28.215, 29.861, 38.264 |
| Unit cell angles | 67.37, 81.44, 79.49 |
Refinement procedure
| Resolution | 21.560 - 1.650 |
| R-factor | 0.165 |
| Rwork | 0.165 |
| R-free | 0.17400 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1hza |
| RMSD bond length | 0.028 |
| RMSD bond angle | 2.100 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | CNS (1.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.710 |
| High resolution limit [Å] | 1.650 | 1.650 |
| Rmerge | 0.031 | 0.095 |
| Number of reflections | 12948 | |
| <I/σ(I)> | 46.9 | 13.9 |
| Completeness [%] | 95.2 | 87.4 |
| Redundancy | 3.9 | 3.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8.2 | 293 | 32% PEG 1500, 0.1M Tris HCl, pH 8.2, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
