5F1B
Structural basis of Ebola virus entry: viral glycoprotein bound to its endosomal receptor Niemann-Pick C1
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 | 2015-06-18 |
Detector | PSI PILATUS 6M |
Wavelength(s) | 0.9793 |
Spacegroup name | P 63 |
Unit cell lengths | 107.261, 107.261, 93.777 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 41.858 - 2.300 |
R-factor | 0.1837 |
Rwork | 0.181 |
R-free | 0.23010 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3csy |
RMSD bond length | 0.008 |
RMSD bond angle | 1.152 |
Data reduction software | HKL-3000 |
Data scaling software | HKL-3000 |
Phasing software | PHASER |
Refinement software | PHENIX (1.8.4_1496) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 50.000 |
High resolution limit [Å] | 2.300 |
Number of reflections | 27329 |
<I/σ(I)> | 32.6 |
Completeness [%] | 100.0 |
Redundancy | 19.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 5.5 | 291 | 15% (v/v) pentaerythritolpropoxylate, 0.2M sodium chloride, pH 5.5, 0.1M MES-NaOH |