2D16
Crystal Structure of PH1918 protein from Pyrococcus horikoshii OT3
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 | 2005-07-20 |
Detector | RIGAKU |
Wavelength(s) | 0.9 |
Spacegroup name | P 3 |
Unit cell lengths | 66.120, 66.120, 125.072 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 33.700 - 1.650 |
R-factor | 0.185 |
Rwork | 0.185 |
R-free | 0.20400 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1vgg |
RMSD bond length | 0.006 |
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] | 40.000 | 1.710 |
High resolution limit [Å] | 1.650 | 1.650 |
Rmerge | 0.066 | |
Number of reflections | 73383 | |
<I/σ(I)> | 7.1 | |
Completeness [%] | 100.0 | 100 |
Redundancy | 5.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | MICROBATCH | 6.3 | 295 | MES-NaOH, PEG 4000, pH 6.3, microbatch, temperature 295.0K |