2B1K
Crystal structure of E. coli CcmG protein
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SEALED TUBE |
| Source details | CONVENTIONAL Cu |
| Temperature [K] | 293 |
| Detector technology | CCD |
| Collection date | 2002-11-21 |
| Detector | BRUKER APEX |
| Wavelength(s) | 1.5418 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 35.483, 48.515, 84.775 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 32.730 - 1.900 |
| R-factor | 0.19 |
| Rwork | 0.190 |
| R-free | 0.21600 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1kng |
| RMSD bond length | 0.005 |
| RMSD bond angle | 1.200 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | CNS |
| Refinement software | CNS (1.0) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.970 |
| High resolution limit [Å] | 1.900 | 1.900 |
| Rmerge | 0.062 | 0.456 |
| Number of reflections | 12145 | |
| Completeness [%] | 99.7 | 97 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.8 | 293 | HEPES buffer, ammonium sulfate, PEG 4000, pH 7.8, VAPOR DIFFUSION, HANGING DROP, temperature 293.0K |
