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 |