5E65
The complex structure of Hemagglutinin-esterase-fusion mutant protein from the influenza D virus with receptor analog 9-O-Ac-3'SLN (Tr322)
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 | 2014-10-01 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 1 |
| Spacegroup name | P 21 3 |
| Unit cell lengths | 164.897, 164.897, 164.897 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 47.602 - 2.200 |
| R-factor | 0.2055 |
| Rwork | 0.203 |
| R-free | 0.24280 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5e5w |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.005 |
| 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 | 2.280 |
| High resolution limit [Å] | 2.199 | 2.200 |
| Rmerge | 0.092 | 0.596 |
| Number of reflections | 75424 | |
| <I/σ(I)> | 24.5 | 3.4 |
| Completeness [%] | 99.6 | 96.5 |
| Redundancy | 9.2 | 7.3 |
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 |
