8JR5
Crystal structure of Hendra Virus attachment(G) glycoprotein mutant S586N
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRF BEAMLINE BL02U1 |
Synchrotron site | SSRF |
Beamline | BL02U1 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2021-06-17 |
Detector | DECTRIS EIGER2 S 9M |
Wavelength(s) | 0.9789 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 83.926, 63.658, 121.622 |
Unit cell angles | 90.00, 97.69, 90.00 |
Refinement procedure
Resolution | 41.590 - 3.300 |
R-factor | 0.2599 |
Rwork | 0.258 |
R-free | 0.29000 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.012 |
RMSD bond angle | 1.589 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHASER |
Refinement software | PHENIX ((1.18.2_3874: ???)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 3.418 |
High resolution limit [Å] | 3.300 | 3.300 |
Number of reflections | 19331 | 19216 |
<I/σ(I)> | 12.68 | |
Completeness [%] | 98.5 | |
Redundancy | 6.2 | |
CC(1/2) | 0.980 | 0.980 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 289 | PEG3350 14%, 10mM MgCl2, 5mM NiCL2, PIPES 6.5 |