2YWO
Crystal structure of reduced thioredoxin-like protein from Thermus thermophilus HB8
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL26B2 |
| Synchrotron site | SPring-8 |
| Beamline | BL26B2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2006-07-21 |
| Detector | RIGAKU JUPITER 210 |
| Wavelength(s) | 1.0000 |
| Spacegroup name | P 41 21 2 |
| Unit cell lengths | 73.490, 73.490, 97.620 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 45.870 - 1.900 |
| R-factor | 0.215 |
| Rwork | 0.215 |
| R-free | 0.23900 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2cvb |
| RMSD bond length | 0.005 |
| RMSD bond angle | 1.300 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | MOLREP |
| Refinement software | CNS (1.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.970 |
| High resolution limit [Å] | 1.900 | 1.900 |
| Rmerge | 0.049 | 0.219 |
| Number of reflections | 21756 | |
| <I/σ(I)> | 59.8 | 12.8 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 13.8 | 14.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 4.6 | 293 | 0.4M Ammonium sulfate, 0.1M Sodium acetate, 32% PEG MME 2000, pH 4.6, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
