1OK7
A Conserved protein binding-site on Bacterial Sliding Clamps
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-4 |
| Synchrotron site | ESRF |
| Beamline | ID14-4 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2002-04-15 |
| Detector | ADSC CCD |
| Spacegroup name | P 1 |
| Unit cell lengths | 41.230, 65.220, 73.380 |
| Unit cell angles | 73.11, 85.58, 85.80 |
Refinement procedure
| Resolution | 20.000 - 1.650 |
| R-factor | 0.203 |
| Rwork | 0.203 |
| R-free | 0.22900 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2pol |
| RMSD bond length | 0.017 |
| RMSD bond angle | 2.100 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | CNS (1.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 1.750 |
| High resolution limit [Å] | 1.650 | 1.650 |
| Rmerge | 0.051 | 0.178 |
| Number of reflections | 85999 | |
| <I/σ(I)> | 12.51 | 5.23 |
| Completeness [%] | 96.7 | 95.6 |
| Redundancy | 2.7 | 2.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 6 | DROPS:0.92 ML OF PROTEIN AT 34.2 MG/ML, 1.89 ML OF P16 AT 1.1 MG/ML, 1 ML OF 2X RESERVOIR SOLUTION. RESERVOIR: 0.1 M MES PH 6.0, 0.1M CACL2 AND 30% PEG 400 |
