7FAV
Crystal Structure of Rubella Protease
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 | 2021-03-12 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 1.28482 |
Spacegroup name | P 43 21 2 |
Unit cell lengths | 60.243, 60.243, 173.860 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 41.370 - 1.640 |
Rwork | 0.180 |
R-free | 0.19880 |
Structure solution method | SAD |
Data reduction software | XDS |
Data scaling software | Aimless (0.7.4) |
Phasing software | CRANK2 |
Refinement software | PHENIX (1.16_3549) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 41.370 | 1.670 |
High resolution limit [Å] | 1.640 | 1.640 |
Rmerge | 0.086 | 1.090 |
Rmeas | 0.087 | |
Rpim | 0.012 | 0.152 |
Number of reflections | 40150 | 3811 |
<I/σ(I)> | 41.82 | |
Completeness [%] | 99.7 | 96.87 |
Redundancy | 51 | 49.8 |
CC(1/2) | 1.000 | 0.912 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 291.15 | 0.1M Hepes pH 7.5, 12.5% Peg 3350 |