2PE3
Crystal structure of Frv operon protein FRVX (PH1821)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 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2004-03-19 |
Detector | RIGAKU RAXIS V |
Wavelength(s) | 1.0 |
Spacegroup name | H 3 |
Unit cell lengths | 125.608, 125.608, 277.323 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 40.670 - 2.000 |
R-factor | 0.166 |
Rwork | 0.166 |
R-free | 0.19700 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1xfo |
RMSD bond length | 0.008 |
RMSD bond angle | 1.400 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | CNS |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.070 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.043 | 0.477 |
Number of reflections | 107669 | |
Completeness [%] | 97.5 | 96 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 6.8 | 293 | 7% PEG 6K, 1M NaCl, pH 6.8, VAPOR DIFFUSION, SITTING DROP, temperature 293K |