3SAM
Structure of D13, the scaffolding protein of vaccinia virus (mutant D513G)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | AUSTRALIAN SYNCHROTRON BEAMLINE MX1 |
Synchrotron site | Australian Synchrotron |
Beamline | MX1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2011-04-16 |
Detector | ADSC QUANTUM 210 |
Wavelength(s) | 0.953689 |
Spacegroup name | P 61 2 2 |
Unit cell lengths | 189.630, 189.630, 255.130 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 17.990 - 2.550 |
R-factor | 0.1763 |
Rwork | 0.175 |
R-free | 0.20080 |
Structure solution method | MIR |
RMSD bond length | 0.010 |
RMSD bond angle | 1.130 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | SHARP |
Refinement software | BUSTER (2.8.0) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 2.620 |
High resolution limit [Å] | 2.550 | 2.550 |
Rmerge | 0.079 | 0.102 |
Number of reflections | 87870 | |
<I/σ(I)> | 26.25 | 2.25 |
Completeness [%] | 99.6 | 99.9 |
Redundancy | 10.9 | 9.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 293 | 2.3M Na formate, 100mM Bis-Tris pH6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |