2CXD
Crystal structure of conserved hypothetical protein, TTHA0068 from Thermus thermophilus HB8
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 | CCD |
Collection date | 2005-05-27 |
Detector | RIGAKU JUPITER 210 |
Wavelength(s) | 0.964 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 54.046, 55.329, 56.702 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 39.600 - 2.000 |
R-factor | 0.192 |
Rwork | 0.192 |
R-free | 0.22900 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2cwy |
RMSD bond length | 0.005 |
RMSD bond angle | 1.100 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | MOLREP |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.090 |
High resolution limit [Å] | 2.000 | 2.000 |
Number of reflections | 12010 | |
<I/σ(I)> | 20.3 | 8 |
Completeness [%] | 99.9 | 99.9 |
Redundancy | 6.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 5.5 | 293 | 0.1M Bis-Tris, 25%(w/v) PEG 3350, pH 5.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K |