3Q4J
Structure of a small peptide ligand bound to E.coli DNA sliding clamp
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SLS BEAMLINE X06SA |
| Synchrotron site | SLS |
| Beamline | X06SA |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2005-06 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 0.9157 |
| Spacegroup name | P 1 |
| Unit cell lengths | 35.090, 132.870, 137.270 |
| Unit cell angles | 62.73, 88.51, 89.77 |
Refinement procedure
| Resolution | 29.520 - 2.300 |
| R-factor | 0.2149 |
| Rwork | 0.214 |
| R-free | 0.25390 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.180 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | BUSTER-TNT (BUSTER 2.8.0) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 30.000 | 30.000 | 2.380 |
| High resolution limit [Å] | 2.300 | 4.950 | 2.300 |
| Rmerge | 0.050 | 0.033 | 0.360 |
| Number of reflections | 96508 | ||
| <I/σ(I)> | 12.2 | ||
| Completeness [%] | 98.6 | 99.1 | 97.9 |
| Redundancy | 3.1 | 3.1 | 3.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION | 6 | 298 | 0.1 M MES PH 6.0, 0.1M CaCl2, 30% PEG 400, vapor diffusion, temperature 298K |
