2IT2
Structure of PH1069 protein from Pyrococcus horikoshii
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SPRING-8 BEAMLINE BL26B1 |
Synchrotron site | SPring-8 |
Beamline | BL26B1 |
Detector technology | IMAGE PLATE |
Collection date | 2006-04-06 |
Detector | RIGAKU RAXIS V |
Wavelength(s) | 1.0 |
Spacegroup name | P 1 |
Unit cell lengths | 37.428, 53.902, 53.212 |
Unit cell angles | 104.60, 102.90, 109.30 |
Refinement procedure
Resolution | 17.550 - 1.500 |
R-factor | 0.25 |
Rwork | 0.250 |
R-free | 0.26500 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2drv |
RMSD bond length | 0.008 |
RMSD bond angle | 1.400 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | PHASER |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.550 |
High resolution limit [Å] | 1.500 | 1.500 |
Rmerge | 0.054 | |
Number of reflections | 53423 | |
<I/σ(I)> | 21.9 | |
Completeness [%] | 100.0 | 99 |
Redundancy | 3.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | MICROBATCH | 7.5 | 295 | HEPES, KH2PO4, pH 7.5, microbatch, temperature 295K |