2CWC
Crystal structure of ADP-ribosylglycohydrolase-related protein 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 | 2005-04-11 |
Detector | RIGAKU JUPITER 210 |
Wavelength(s) | 1.00000 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 44.212, 73.943, 78.925 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 27.350 - 1.650 |
R-factor | 0.193 |
Rwork | 0.193 |
R-free | 0.21400 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.004 |
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 | 1.710 |
High resolution limit [Å] | 1.650 | 1.650 |
Rmerge | 0.044 | 0.229 |
Number of reflections | 31755 | |
<I/σ(I)> | 43.8 | 4.99 |
Completeness [%] | 99.8 | 99.5 |
Redundancy | 6.9 | 6.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 8 | 293 | 17% PEG6000, 0.1M Tris, 0.1M diammonium hydrogen phosphate, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K |