1V8C
Crystal Structure of MoaD 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 | IMAGE PLATE |
Collection date | 2003-11-04 |
Detector | RIGAKU RAXIS V |
Wavelength(s) | 1.00 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 80.179, 83.553, 93.066 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 30.000 - 1.600 |
R-factor | 0.221 |
Rwork | 0.221 |
R-free | 0.24700 |
Structure solution method | MIR |
RMSD bond length | 0.005 |
RMSD bond angle | 1.200 |
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] | 30.000 | 1.660 |
High resolution limit [Å] | 1.600 | 1.600 |
Rmerge | 0.050 | 0.428 |
Number of reflections | 82859 | |
<I/σ(I)> | 16.5 | 5.44 |
Completeness [%] | 100.0 | 100 |
Redundancy | 7.6 | 7.64 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | MICROBATCH | 4.7 | 295 | 10mM Cobaltous Chlodide, 100mM Sodium Acetate, 1.0M 1,6-Hexanediol, pH 4.7, microbatch, temperature 295K |