2IIH
Crystal structure of the molybdenum cofactor biosynthesis protein C (TTHA1789) from thermus theromophilus HB8 (H32 form)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 22-BM |
Synchrotron site | APS |
Beamline | 22-BM |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2006-08-24 |
Detector | MARMOSAIC 225 mm CCD |
Wavelength(s) | 0.97243 |
Spacegroup name | H 3 2 |
Unit cell lengths | 106.573, 106.573, 59.251 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 23.500 - 1.750 |
R-factor | 0.196 |
Rwork | 0.196 |
R-free | 0.21700 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2ide |
RMSD bond length | 0.004 |
RMSD bond angle | 1.400 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | PHASER |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.810 |
High resolution limit [Å] | 1.750 | 1.750 |
Rmerge | 0.096 | 0.175 |
Number of reflections | 13115 | |
Completeness [%] | 99.9 | 100 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 5 | 293 | 0.1M Na Acetate, 1.0M Ammonium H2 phosphate, pH 5.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K |