2EKQ
Structure of TT0495 protein from Thermus thermophilus
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 41 21 2 |
Unit cell lengths | 110.531, 110.531, 200.851 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 32.490 - 1.800 |
R-factor | 0.18 |
Rwork | 0.180 |
R-free | 0.20800 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1x1e |
RMSD bond length | 0.004 |
RMSD bond angle | 1.200 |
Data reduction software | HKL-2000 |
Data scaling software | SCALA |
Phasing software | CNS |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 40.000 | 1.860 |
High resolution limit [Å] | 1.800 | 1.800 |
Rmerge | 0.066 | |
Number of reflections | 114536 | |
<I/σ(I)> | 10.5 | |
Completeness [%] | 99.9 | 100 |
Redundancy | 5.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 9.4 | 295 | 22% PEG 2000, 0.3M NH2SO4, pH 9.4, VAPOR DIFFUSION, SITTING DROP, temperature 295K |