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 |