6LS9
Crystal structure of bovine herpesvirus 1 glycoprotein D
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 | 2018-05-01 |
Detector | DECTRIS PILATUS3 S 6M |
Wavelength(s) | 1.03645 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 116.272, 104.392, 98.772 |
Unit cell angles | 90.00, 112.50, 90.00 |
Refinement procedure
Resolution | 37.433 - 2.503 |
R-factor | 0.2072 |
Rwork | 0.205 |
R-free | 0.24330 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5x5v |
RMSD bond length | 0.012 |
RMSD bond angle | 1.205 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHASER |
Refinement software | PHENIX (1.10.1_2155) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.590 |
High resolution limit [Å] | 2.500 | 2.500 |
Rmerge | 0.110 | 0.573 |
Number of reflections | 37572 | 3702 |
<I/σ(I)> | 21.111 | |
Completeness [%] | 99.8 | |
Redundancy | 6.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 8 | 291 | 0.2M Ammonium acetate, 0.1M Tris-HCl, 16% w/v Polyethylene glycol 10000 |