2EF0
Crystal structure of ornithine carbamoyltransferase from thermus thermophilus
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SPRING-8 BEAMLINE BL26B2 |
Synchrotron site | SPring-8 |
Beamline | BL26B2 |
Temperature [K] | 180 |
Detector technology | CCD |
Collection date | 2006-10-04 |
Detector | RIGAKU JUPITER 210 |
Wavelength(s) | 1.000 |
Spacegroup name | P 63 |
Unit cell lengths | 77.385, 77.385, 79.132 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 19.780 - 2.000 |
R-factor | 0.2 |
Rwork | 0.200 |
R-free | 0.23600 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1pvv |
RMSD bond length | 0.006 |
RMSD bond angle | 1.400 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | MOLREP |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.070 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.096 | 0.535 |
Number of reflections | 18296 | |
Completeness [%] | 100.0 | 100 |
Redundancy | 10.6 | 100 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 293 | 10% PEG 4000, 0.1M NaCl, 0.1M Hepas-NA, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K |