3TS3
Crystal structure of the projection domain of the turkey astrovirus capsid protein at 1.5 angstrom resolution
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 22-BM |
| Synchrotron site | APS |
| Beamline | 22-BM |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2011-08-24 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 1.0 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 44.487, 127.878, 71.007 |
| Unit cell angles | 90.00, 104.49, 90.00 |
Refinement procedure
| Resolution | 50.000 - 1.490 |
| R-factor | 0.1776 |
| Rwork | 0.176 |
| R-free | 0.20530 |
| Structure solution method | SAD |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.179 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | SOLVE |
| Refinement software | REFMAC (5.5.0102) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 1.540 |
| High resolution limit [Å] | 1.490 | 3.210 | 1.490 |
| Rmerge | 0.066 | 0.030 | 0.391 |
| Number of reflections | 124746 | ||
| <I/σ(I)> | 8.8 | ||
| Completeness [%] | 99.9 | 99.8 | 99.2 |
| Redundancy | 5.8 | 6 | 4.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8 | 291 | PEG 4000, ammonium sulfate, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 291K |
