6CY9
SA11 Rotavirus NSP2 with disulfide bridge
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 8.2.1 |
| Synchrotron site | ALS |
| Beamline | 8.2.1 |
| Temperature [K] | 80 |
| Detector technology | CCD |
| Collection date | 2017-10-11 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.999949 |
| Spacegroup name | I 4 2 2 |
| Unit cell lengths | 107.224, 107.224, 149.700 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 45.241 - 2.615 |
| R-factor | 0.2024 |
| Rwork | 0.201 |
| R-free | 0.23540 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1l9v |
| RMSD bond length | 0.004 |
| RMSD bond angle | 0.807 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | PHENIX ((1.13_2998: ???)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 45.241 | 2.640 |
| High resolution limit [Å] | 2.615 | 2.600 |
| Rmerge | 0.136 | 1.480 |
| Rpim | 0.036 | 0.390 |
| Number of reflections | 13423 | |
| <I/σ(I)> | 22.3 | |
| Completeness [%] | 99.1 | |
| Redundancy | 15.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 293.15 | 5 mg/mL protein, 0.16 M calcium acetate, 0.08 M sodium cacodylate, 14.4% polyethylene glycol, 20% glycerol |
