2DRV
Structure of PH1069 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 | 2006-03-16 |
Detector | RIGAKU RAXIS V |
Wavelength(s) | 0.979141, 0.97341, 1.0 |
Spacegroup name | P 1 |
Unit cell lengths | 37.346, 52.898, 53.125 |
Unit cell angles | 104.65, 102.96, 109.25 |
Refinement procedure
Resolution | 36.820 - 1.600 |
R-factor | 0.218 |
Rwork | 0.218 |
R-free | 0.24500 |
Structure solution method | MAD |
RMSD bond length | 0.008 |
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] | 40.000 | 1.660 |
High resolution limit [Å] | 1.600 | 1.600 |
Rmerge | 0.065 | |
Number of reflections | 43824 | |
<I/σ(I)> | 14.7 | |
Completeness [%] | 100.0 | 90.2 |
Redundancy | 3.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | MICROBATCH | 4.6 | 295 | Sodium acetate, Ammonium sulfate, pH 4.6, MICROBATCH, temperature 295.0K |