1EO8
INFLUENZA VIRUS HEMAGGLUTININ COMPLEXED WITH A NEUTRALIZING ANTIBODY
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID2 |
Synchrotron site | ESRF |
Beamline | ID2 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 1995-11-10 |
Detector | MARRESEARCH |
Spacegroup name | P 3 2 1 |
Unit cell lengths | 138.150, 138.150, 129.500 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 7.000 - 2.800 |
R-factor | 0.196 * |
Rwork | 0.196 |
R-free | 0.29800 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.013 |
RMSD bond angle | 1.900 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | X-PLOR (3.843) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 25.000 | 2.850 |
High resolution limit [Å] | 2.800 | 2.800 |
Rmerge | 0.068 | 0.336 |
Total number of observations | 186998 * | |
Number of reflections | 49210 | |
<I/σ(I)> | 7.5 | |
Completeness [%] | 99.0 | 99 |
Redundancy | 3.8 | 3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8.5 * | 18 * | Gigant, B., (1995) Proteins: Struct., Funct., Genet., 23, 115. * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 10-15 (mg/ml) | |
2 | 1 | reservoir | PEG2000 | 10 (%(w/v)) | |
3 | 1 | reservoir | Tris-HCl | 100 (mM) | |
4 | 1 | reservoir | 150 (mM) | ||
5 | 1 | reservoir | 0.05 (%(w/v)) | ||
6 | 1 | drop | 150 (mM) |