3SYL
Crystal structure of the AAA+ protein CbbX, native structure
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 | 2009-07-26 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 1.0000 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 76.128, 93.141, 106.102 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 20.000 - 3.000 |
| R-factor | 0.2218 |
| Rwork | 0.218 |
| R-free | 0.28540 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3syk |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.084 |
| Data reduction software | XDS |
| Data scaling software | SCALA (3.2.25) |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 46.098 | 46.098 | 3.160 |
| High resolution limit [Å] | 2.894 | 9.490 | 3.000 |
| Rmerge | 0.078 | 0.015 | 0.453 |
| Total number of observations | 1799 | 8278 | |
| Number of reflections | 15101 | ||
| <I/σ(I)> | 15 | 42.1 | 1.7 |
| Completeness [%] | 96.9 | 93.6 | 97.8 |
| Redundancy | 3.7 | 3.5 | 3.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION | 6.5 | 291 | 0.4 M (NH4)2SO4, 0.05 M MES-NaOH pH 6.5, vapor diffusion, temperature 291K |
