2VQ0
Capsid structure of Sesbania mosaic virus coat protein deletion mutant rCP(delta 48 to 59)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU RU200 |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Detector | MARRESEARCH |
| Spacegroup name | R 3 |
| Unit cell lengths | 288.793, 288.793, 288.793 |
| Unit cell angles | 61.70, 61.70, 61.70 |
Refinement procedure
| Resolution | 20.000 - 3.600 |
| R-factor | 0.2567 |
| Rwork | 0.257 |
| R-free | 0.25840 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1x33 |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.457 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | GLRF |
| Refinement software | CNS (1.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 3.730 |
| High resolution limit [Å] | 3.600 | 3.600 |
| Rmerge | 0.170 | 0.480 |
| Number of reflections | 262266 | |
| <I/σ(I)> | 5.7 | 1.8 |
| Completeness [%] | 99.3 | 99 |
| Redundancy | 2.89 | 2.36 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 0.2 M LI2SO4 MONOHYDRATE, 0.1 M BISTRIS (PH7.5), 25 % PEG 3350 VAPOUR DIFFUSION, SITTING DROP |
