2CW5
Crystal structure of a conserved hypothetical protein from Thermus thermophilus HB8
Experimental procedure
Experimental method | MAD |
Source type | SYNCHROTRON |
Source details | SPRING-8 BEAMLINE BL26B2 |
Synchrotron site | SPring-8 |
Beamline | BL26B2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2004-10-11 |
Detector | RIGAKU JUPITER 210 |
Wavelength(s) | 0.90000, 0.97906, 0.97941 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 74.790, 78.120, 120.580 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 37.400 - 1.940 |
R-factor | 0.212 |
Rwork | 0.212 |
R-free | 0.24600 |
Structure solution method | MAD |
RMSD bond length | 0.005 |
RMSD bond angle | 1.300 |
Data reduction software | CrystalClear |
Data scaling software | CrystalClear |
Phasing software | SOLVE |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 40.000 | 2.010 |
High resolution limit [Å] | 1.940 | 1.940 |
Rmerge | 0.062 | 0.313 |
<I/σ(I)> | 14.2 | 5.4 |
Completeness [%] | 99.6 | 100 |
Redundancy | 7.12 | 7.23 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 293 | 1.4M Mg sulfate, 0.1M MES, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K |