3AL4
Crystal structure of the swine-origin A (H1N1)-2009 influenza A virus hemagglutinin (HA) reveals similar antigenicity to that of the 1918 pandemic virus
Replaces: 3LYJExperimental 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 | 2010-01-23 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 0.9795 |
| Spacegroup name | P 1 |
| Unit cell lengths | 66.020, 115.190, 114.985 |
| Unit cell angles | 62.31, 77.94, 81.05 |
Refinement procedure
| Resolution | 24.190 - 2.872 |
| R-factor | 0.247 |
| Rwork | 0.246 |
| R-free | 0.27000 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1ru7 |
| RMSD bond length | 0.004 |
| RMSD bond angle | 0.971 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | PHENIX ((PHENIX.REFINE: 1.5_2)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 3.000 |
| High resolution limit [Å] | 2.872 | 2.870 |
| Rmerge | 0.105 | 0.501 |
| Number of reflections | 64796 | |
| <I/σ(I)> | 12.9 | 1.9 |
| Completeness [%] | 98.0 | 90.7 |
| Redundancy | 3.7 | 2.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 291 | 10% PEG 6000, 5% MPD, 0.1M MES, PH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K |
