1WEK
Crystal structure of the conserved hypothetical protein TT1465 from Thermus thermophilus HB8
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 | CCD |
Collection date | 2004-04-03 |
Detector | MARRESEARCH |
Wavelength(s) | 0.979099, 0.979377, 0.974000 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 65.650, 83.798, 265.143 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 14.940 - 2.200 |
R-factor | 0.198 |
Rwork | 0.198 |
R-free | 0.25000 |
Structure solution method | MAD |
RMSD bond length | 0.008 |
RMSD bond angle | 1.500 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | SOLVE |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.280 |
High resolution limit [Å] | 2.200 | 2.200 |
Number of reflections | 70481 | |
<I/σ(I)> | 16.5034 | 3.46074 |
Completeness [%] | 92.5 | 79.1 |
Redundancy | 7.05944 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | VAPOR DIFFUSION, HANGING DROP |