3SYK
Crystal structure of the AAA+ protein CbbX, selenomethionine structure
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID23-1 |
| Synchrotron site | ESRF |
| Beamline | ID23-1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2009-12-16 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.97915 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 76.770, 93.993, 106.964 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 20.000 - 3.080 |
| R-factor | 0.2229 |
| Rwork | 0.220 |
| R-free | 0.28320 |
| Structure solution method | SAD |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.076 |
| Data reduction software | XDS |
| Data scaling software | SCALA (3.3.9) |
| Phasing software | SHELX |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 43.883 | 43.883 | 3.250 |
| High resolution limit [Å] | 3.081 | 9.740 | 3.080 |
| Rmerge | 0.022 | 0.322 | |
| Total number of observations | 1701 | 7304 | |
| Number of reflections | 14768 | ||
| <I/σ(I)> | 13.1 | 28.2 | 2.4 |
| Completeness [%] | 99.2 | 98.5 | 95.2 |
| Redundancy | 3.6 | 3.2 | 3.6 |
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 |
