8P61
Crystal structure of O'nyong'nyong virus capsid protease (106-256)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | PETRA III, DESY BEAMLINE P11 |
Synchrotron site | PETRA III, DESY |
Beamline | P11 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2022-11-01 |
Detector | DECTRIS EIGER X 16M |
Wavelength(s) | 1.0332 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 89.650, 112.130, 67.100 |
Unit cell angles | 90.00, 89.97, 90.00 |
Refinement procedure
Resolution | 44.865 - 1.900 |
Rwork | 0.225 |
R-free | 0.26800 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.008 |
RMSD bond angle | 1.588 |
Data reduction software | XDS |
Data scaling software | Aimless |
Phasing software | PHASER |
Refinement software | REFMAC (5.8.0403) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 48.460 | 1.940 |
High resolution limit [Å] | 1.900 | 1.900 |
Number of reflections | 51622 | 3314 |
<I/σ(I)> | 2.5 | 0.6 |
Completeness [%] | 98.9 | |
Redundancy | 1.7 | |
CC(1/2) | 0.961 | 0.157 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 293.15 | 0.1 M sodium cacodylate (pH 6.5), 2.2 M ammonium sulfate and 100 mM ethylenediaminetetraacetic acid disodium salt Crystals were cryoprotected in 25% (v/v) glycerol in the reservoir solution and flash-cooled in liquid nitrogen |