3O2R
Structural flexibility in region involved in dimer formation of nuclease domain of Ribonuclase III (rnc) from Campylobacter jejuni
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 21-ID-G |
| Synchrotron site | APS |
| Beamline | 21-ID-G |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2010-06-03 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 0.97856 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 38.451, 61.552, 118.093 |
| Unit cell angles | 90.00, 90.09, 90.00 |
Refinement procedure
| Resolution | 29.780 - 1.251 |
| R-factor | 0.13501 |
| Rwork | 0.133 |
| R-free | 0.16830 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3n3w |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.287 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.5.0102) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 1.270 |
| High resolution limit [Å] | 1.250 | 1.250 |
| Rmerge | 0.062 | 0.359 |
| Number of reflections | 151202 | |
| <I/σ(I)> | 16.4 | 2.6 |
| Completeness [%] | 99.6 | 99.4 |
| Redundancy | 3 | 2.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 4 | 295 | Protein solution: 7.6 mg/mL, 0.5M Sodium chloride, 0.01M Tris pH 8.3; Screen solution: PACT (B1), 0.1M MIB buffer pH 4.0, 25% w/v PEG1500, VAPOR DIFFUSION, SITTING DROP, temperature 295K |
