1KHY
The Crystal Structure of ClpB N Terminal Domain, Implication to the Peptide Binding Function of ClpB
Experimental procedure
| Experimental method | MAD |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 14-BM-C |
| Synchrotron site | APS |
| Beamline | 14-BM-C |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2001-02-17 |
| Detector | ADSC QUANTUM 4 |
| Wavelength(s) | 1.01, 0.9785, 0.9781, 0.9556 |
| Spacegroup name | P 1 |
| Unit cell lengths | 50.213, 52.600, 56.841 |
| Unit cell angles | 90.45, 111.73, 107.05 |
Refinement procedure
| Resolution | 30.000 - 1.950 |
| R-factor | 0.226 |
| Rwork | 0.222 |
| R-free | 0.25900 |
| Structure solution method | MAD |
| RMSD bond length | 0.005 |
| RMSD bond angle | 1.100 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | SOLVE |
| Refinement software | CNS (1.0) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 2.040 |
| High resolution limit [Å] | 1.950 | 1.950 |
| Rmerge | 0.050 | 0.128 |
| Number of reflections | 35923 | |
| <I/σ(I)> | 24.4 | 11.2 |
| Completeness [%] | 93.9 | |
| Redundancy | 1.6 | 2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 277 | PEG 20K, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K |
