1VE3
Crystal structure of PH0226 protein from Pyrococcus horikoshii OT3
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 | 2004-02-28 |
Detector | RIGAKU RAXIS V |
Wavelength(s) | 0.97882, 0.97945, 1.0 |
Spacegroup name | P 32 2 1 |
Unit cell lengths | 58.167, 58.167, 252.463 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 29.330 - 2.100 |
R-factor | 0.236 |
Rwork | 0.236 |
R-free | 0.27000 |
Structure solution method | MAD |
RMSD bond length | 0.007 |
RMSD bond angle | 1.300 |
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 | 2.180 |
High resolution limit [Å] | 2.100 | 2.100 |
Rmerge | 0.049 | |
Number of reflections | 29753 | |
Completeness [%] | 99.9 | 99.6 |
Redundancy | 5.2 | 5.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | MICROBATCH | 4.6 | 295 | PEG 4K, Na acetate, pH 4.6, microbatch, temperature 295.0K |