2XVX
Cobalt chelatase CbiK (periplasmatic) from Desulvobrio vulgaris Hildenborough (Native)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-1 |
| Synchrotron site | ESRF |
| Beamline | ID14-1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2007-04-20 |
| Detector | ADSC CCD |
| Spacegroup name | I 4 2 2 |
| Unit cell lengths | 121.062, 121.062, 120.246 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 85.600 - 1.900 |
| R-factor | 0.17477 |
| Rwork | 0.174 |
| R-free | 0.19875 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | MODEL OBTAINED WITH THE PROTEIN CO- CRYSTALLIZED WITH COBALT. |
| RMSD bond length | 0.020 |
| RMSD bond angle | 1.767 |
| Data reduction software | XDS |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.5.0063) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 42.800 | 2.000 |
| High resolution limit [Å] | 1.900 | 1.900 |
| Rmerge | 0.080 | 0.830 |
| Number of reflections | 35365 | |
| <I/σ(I)> | 7.6 | 0.9 |
| Completeness [%] | 99.9 | 99.2 |
| Redundancy | 28 | 20.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 8.5 | CRYSTALLIZATION SOLUTION: 100MM TRIS-HCL PH8.5, 2M AMMONIUM SULFATE. THE DROP WAS MADE BY ADDING 1UL OF PROTEIN PLUS 2UL OF CRYSTALLIZATION SOLUTION. |
