2VED
crystal structure of the chimerical mutant CapABK55M protein
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID29 |
| Synchrotron site | ESRF |
| Beamline | ID29 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2007-05-19 |
| Detector | ADSC QUANTUM 315r |
| Spacegroup name | I 4 |
| Unit cell lengths | 163.200, 163.200, 57.200 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 19.790 - 2.600 |
| R-factor | 0.208 |
| Rwork | 0.204 |
| R-free | 0.27000 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1ion |
| RMSD bond length | 0.017 |
| RMSD bond angle | 1.870 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 2.700 |
| High resolution limit [Å] | 2.600 | 2.600 |
| Rmerge | 0.150 | 0.590 |
| Number of reflections | 23263 | |
| <I/σ(I)> | 8 | 1.9 |
| Completeness [%] | 99.4 | 96.4 |
| Redundancy | 4 | 3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 7.5 | 20% PEG1000 100MM HEPES PH7.5 200MM GLYCINE |
