3SAQ
Structure of D13, the scaffolding protein of vaccinia virus
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | AUSTRALIAN SYNCHROTRON BEAMLINE MX2 |
| Synchrotron site | Australian Synchrotron |
| Beamline | MX2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2010-02-25 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.95369 |
| Spacegroup name | H 3 2 |
| Unit cell lengths | 125.130, 125.130, 370.830 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 26.810 - 3.510 |
| R-factor | 0.2457 |
| Rwork | 0.245 |
| R-free | 0.25650 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2sam |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.090 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | BUSTER (2.8.0) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 3.620 |
| High resolution limit [Å] | 3.500 | 3.500 |
| Rmerge | 0.156 | 0.557 |
| Number of reflections | 13943 | |
| <I/σ(I)> | 10.4 | 2.19 |
| Completeness [%] | 97.9 | 98.8 |
| Redundancy | 6.8 | 6.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8 | 200mM NaBr, 20% PEG3550, Tris pH 8.0, VAPOR DIFFUSION, HANGING DROP |
