2OJ5
Crystal Structure of Reovirus T3D Attachment Protein Sigma1 head domain wild-type at 1.75 A resolution
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X29A |
| Synchrotron site | NSLS |
| Beamline | X29A |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2004-01-01 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 1.1 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 83.927, 51.381, 108.870 |
| Unit cell angles | 90.00, 95.66, 90.00 |
Refinement procedure
| Resolution | 30.000 - 1.750 |
| R-factor | 0.23222 |
| Rwork | 0.228 |
| R-free | 0.27373 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | residues 293-455 of 1KKE |
| RMSD bond length | 0.008 |
| RMSD bond angle | 0.963 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 1.810 |
| High resolution limit [Å] | 1.750 | 1.750 |
| Rmerge | 0.093 | 0.427 |
| Number of reflections | 90611 | |
| <I/σ(I)> | 15.71 | 2.26 |
| Completeness [%] | 96.7 | 86.7 |
| Redundancy | 3.3 | 2.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.9 | 293 | 0.1 M sodium cacodylate, 0.2 M magnesium sulfate, 10-12% PEG 8000; protein concentration 13.6 mg/ml, pH 6.9, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
