5E66
The complex structure of Hemagglutinin-esterase-fusion mutant protein from the influenza D virus with receptor analog 9-N-Ac-Sia
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRF BEAMLINE BL17U |
| Synchrotron site | SSRF |
| Beamline | BL17U |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2014-06-03 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 1 |
| Spacegroup name | I 21 3 |
| Unit cell lengths | 165.297, 165.297, 165.297 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 38.961 - 3.100 |
| R-factor | 0.2351 |
| Rwork | 0.234 |
| R-free | 0.26530 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5e64 |
| RMSD bond length | 0.013 |
| RMSD bond angle | 1.540 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.9_1692) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 3.210 |
| High resolution limit [Å] | 3.100 | 3.100 |
| Rmerge | 0.079 | 0.858 |
| Number of reflections | 13867 | |
| <I/σ(I)> | 23.3 | 2.4 |
| Completeness [%] | 99.9 | 100 |
| Redundancy | 7.2 | 7.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 291 | 0.1M PCTP (Propionic acid, Cacodylate, Bis-tris propane system) buffer pH 8.5, 22.5 % w/v PEG 1500 |
