1EA3
Influenza virus M1 protein
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-1 |
Synchrotron site | ESRF |
Beamline | ID14-1 |
Temperature [K] | 90 |
Detector technology | CCD |
Collection date | 2000-07-15 |
Detector | MARRESEARCH |
Spacegroup name | P 1 |
Unit cell lengths | 36.860, 44.147, 47.692 |
Unit cell angles | 77.10, 67.83, 77.60 |
Refinement procedure
Resolution | 14.980 - 2.300 |
R-factor | 0.242 |
Rwork | 0.242 |
R-free | 0.31300 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1aa7 |
RMSD bond length | 0.007 |
RMSD bond angle | 17.900 * |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | AMoRE |
Refinement software | CNS (1.0) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 33.150 | 2.390 |
High resolution limit [Å] | 2.300 | 2.300 |
Rmerge | 0.067 * | 0.212 * |
Number of reflections | 11585 | |
<I/σ(I)> | 5.3 | 2.6 |
Completeness [%] | 97.1 | 97.1 |
Redundancy | 3.8 | 3.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 7.5 * | drop contains protein and reservoir solution in a 1:1 ratio * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 14 (mg/ml) | |
2 | 1 | drop | Tris-HCl | 10 (mM) | |
3 | 1 | drop | 100 (mM) | ||
4 | 1 | drop | mercaptoethanol | 10 (mM) | |
5 | 1 | reservoir | HEPES | 0.1 (M) | |
6 | 1 | reservoir | isopropanol | 5 (%(v/v)) | |
7 | 1 | reservoir | PEG4000 | 6-10 (%) |