6LUS
Crystal structure of the Mengla Virus VP30 C-terminal domain
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRF BEAMLINE BL19U1 |
Synchrotron site | SSRF |
Beamline | BL19U1 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2019-06-06 |
Detector | DECTRIS PILATUS3 S 6M |
Wavelength(s) | 0.97852 |
Spacegroup name | P 32 1 2 |
Unit cell lengths | 73.886, 73.886, 53.405 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 30.401 - 1.400 |
Rwork | 0.177 |
R-free | 0.18220 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5t3w |
RMSD bond length | 0.017 |
RMSD bond angle | 1.837 |
Data reduction software | HKL-3000 |
Data scaling software | HKL-3000 |
Phasing software | PHASER |
Refinement software | REFMAC (5.8.0258) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.420 |
High resolution limit [Å] | 1.400 | 1.400 |
Number of reflections | 32952 | 1628 |
<I/σ(I)> | 56.96 | |
Completeness [%] | 100.0 | |
Redundancy | 19.9 | |
CC(1/2) | 0.995 | 0.965 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 289.15 | Citric acid, Polyethylene glycol 3350 |