2IDE
Crystal Structure of the molybdenum cofactor biosynthesis protein C (TTHA1789) from Thermus Theromophilus HB8
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SPRING-8 BEAMLINE BL26B2 |
Synchrotron site | SPring-8 |
Beamline | BL26B2 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2006-07-07 |
Detector | RIGAKU |
Wavelength(s) | 1.0000 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 64.809, 109.836, 115.192 |
Unit cell angles | 90.00, 104.86, 90.00 |
Refinement procedure
Resolution | 49.660 - 1.900 |
R-factor | 0.195 |
Rwork | 0.195 |
R-free | 0.22600 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1ekr |
RMSD bond length | 0.005 |
RMSD bond angle | 1.500 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | CNS |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.970 |
High resolution limit [Å] | 1.900 | 1.900 |
Rmerge | 0.042 | 0.174 |
Number of reflections | 121501 | |
Completeness [%] | 99.9 | 99.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 4.2 | 293 | 25%, 1,2-propanediol, 5% PEG3000, 0.1M phosphate-citrate pH 4.2, 10% Glycerol, VAPOR DIFFUSION, SITTING DROP, temperature 293K |