2EKN
Structure of PH1811 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 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2006-12-13 |
Detector | RIGAKU |
Wavelength(s) | 1.0 |
Spacegroup name | P 31 2 1 |
Unit cell lengths | 119.910, 119.910, 63.960 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 40.000 - 2.050 |
R-factor | 0.19 |
Rwork | 0.190 |
R-free | 0.21000 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1ekr |
RMSD bond length | 0.005 |
RMSD bond angle | 1.300 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | CNS |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.120 |
High resolution limit [Å] | 2.050 | 2.050 |
Rmerge | 0.098 | |
Number of reflections | 33087 | |
<I/σ(I)> | 6.6 | |
Completeness [%] | 100.0 | 99.9 |
Redundancy | 5.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 295 | 30% PEG 8000, 0.5M LiCl, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 295K |