4JCX
Crystal structure of the Restriction-Modification Controller Protein C.Csp231I OL operator complex
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-4 |
| Synchrotron site | ESRF |
| Beamline | ID14-4 |
| Temperature [K] | 120 |
| Detector technology | CCD |
| Collection date | 2010-11-23 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.93930 |
| Spacegroup name | P 61 |
| Unit cell lengths | 62.200, 62.200, 147.800 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 50.610 - 2.300 |
| R-factor | 0.17309 |
| Rwork | 0.172 |
| R-free | 0.19647 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3lfp |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.036 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.7.0029) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.610 | 2.390 |
| High resolution limit [Å] | 2.300 | 2.300 |
| Rmerge | 0.111 | 0.557 |
| Number of reflections | 14402 | |
| <I/σ(I)> | 10.5 | 3.2 |
| Completeness [%] | 99.9 | 100 |
| Redundancy | 6 | 6.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 289 | Protein was dialysed against the buffer containing 0.1 M NaCl, 50 mM TRIS-HCl, pH 8.2, 1 mM DTT and 1 mM EDTA. Crystallisation conditions: 0.2 M ammonium chloride, 0.1 M MES pH 6.0, 20 % (w/v) PEG6K, protein dimer/DNA molar ratio 1:2, protein concentration 1.2 mg/ml, VAPOR DIFFUSION, SITTING DROP, temperature 289K |






