4Y4Y
T=1 capsid structure of SeMV Ndel65CP fused with B-domain of S. aureus protein SpA at the N-terminus (C2 crystal form)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE BM14 |
| Synchrotron site | ESRF |
| Beamline | BM14 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2012-08-01 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 0.95372 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 288.181, 193.040, 189.192 |
| Unit cell angles | 90.00, 124.37, 90.00 |
Refinement procedure
| Resolution | 50.000 - 3.000 |
| R-factor | 0.1802 |
| Rwork | 0.179 |
| R-free | 0.19960 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1vak |
| RMSD bond length | 0.015 |
| RMSD bond angle | 1.524 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0049) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 3.050 |
| High resolution limit [Å] | 3.000 | 8.130 | 3.000 |
| Rmerge | 0.036 | 0.730 | |
| Total number of observations | 863389 | ||
| Number of reflections | 169159 | ||
| <I/σ(I)> | 6.3 | 2.5 | |
| Completeness [%] | 100.0 | 99.7 | 100 |
| Redundancy | 5.1 | 5 | 4.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 295 | 15-20% PEG 4000, 5% Iso-propanol, 100 mM Sodium citrate |
