1V5V
Crystal Structure of a Component of Glycine Cleavage System: T-protein from Pyrococcus horikoshii OT3 at 1.5 A Resolution
Experimental procedure
| Experimental method | MAD |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL26B1 |
| Synchrotron site | SPring-8 |
| Beamline | BL26B1 |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2003-10-17 |
| Detector | RIGAKU RAXIS |
| Wavelength(s) | 2.0, 0.91971, 0.92001, 0.92540 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 79.496, 96.099, 118.605 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 28.500 - 1.500 |
| R-factor | 0.197 |
| Rwork | 0.197 |
| R-free | 0.20900 |
| Structure solution method | MAD |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.400 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | SOLVE |
| Refinement software | CNS (1.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 1.550 |
| High resolution limit [Å] | 1.500 | 1.500 |
| Rmerge | 0.049 | |
| Number of reflections | 141020 | |
| Completeness [%] | 97.3 | 96.8 |
| Redundancy | 6.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | MICROBATCH | 5.9 | 295 | PEG, MES, pH 5.9, MICROBATCH, temperature 295K |






