2ZKT
Structure of PH0037 protein from Pyrococcus horikoshii
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 | 2005-05-21 |
Detector | RIGAKU |
Wavelength(s) | 1.282247, 1.282786, 1.33 |
Spacegroup name | H 3 2 |
Unit cell lengths | 155.900, 155.900, 230.857 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 10.000 - 2.400 |
R-factor | 0.27749 |
Rwork | 0.277 |
R-free | 0.28556 |
Structure solution method | MAD |
RMSD bond length | 0.011 |
RMSD bond angle | 1.440 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | SOLVE |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 50.000 |
High resolution limit [Å] | 2.400 |
Rmerge | 0.062 |
Number of reflections | 39476 |
<I/σ(I)> | 10.2 |
Completeness [%] | 99.9 |
Redundancy | 4.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION | 6.6 | 295 | 18% PEG 20K, 0.1M Tris_Hcl, 0.5M licl2, pH 6.6, VAPOR DIFFUSION, temperature 295K |