3GQ0
The structure of the Caulobacter crescentus clpS protease adaptor protein - apo structure with no peptide
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 24-ID-E |
| Synchrotron site | APS |
| Beamline | 24-ID-E |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2009-02-26 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.97918 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 27.667, 38.479, 62.560 |
| Unit cell angles | 90.00, 88.42, 90.00 |
Refinement procedure
| Resolution | 32.772 - 2.066 |
| R-factor | 0.223 |
| Rwork | 0.221 |
| R-free | 0.26400 |
| Starting model (for MR) | 3dnj |
| RMSD bond length | 0.004 |
| RMSD bond angle | 0.712 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Refinement software | PHENIX |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 2.140 |
| High resolution limit [Å] | 2.100 | 5.700 | 2.100 |
| Rmerge | 0.141 | 0.095 | 0.435 |
| Number of reflections | 7983 | ||
| <I/σ(I)> | 22.816 | ||
| Completeness [%] | 98.2 | 98.8 | 94.5 |
| Redundancy | 10.5 | 10.5 | 8.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION | 5.5 | 300 | 0.1 M bis-tris pH 5.5, 0.025 M MgCl2, 14% PEG 3350, vapor diffusion, temperature 300K |
