2ALA
Crystal structure of the Semliki Forest Virus envelope protein E1 in its monomeric conformation.
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE BM14 |
Synchrotron site | ESRF |
Beamline | BM14 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 1998-09-29 |
Wavelength(s) | 0.945 |
Spacegroup name | P 64 2 2 |
Unit cell lengths | 79.380, 79.380, 335.910 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 39.000 - 3.000 |
R-factor | 0.27199 |
Rwork | 0.267 |
R-free | 0.31800 * |
Structure solution method | MIR |
RMSD bond length | 0.006 |
RMSD bond angle | 1.028 * |
Data reduction software | MOSFLM |
Data scaling software | SCALEPACK |
Phasing software | MLPHARE |
Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 39.000 | 3.210 |
High resolution limit [Å] | 3.000 | 3.000 |
Rmerge | 0.075 | 0.124 |
Total number of observations | 82854 * | |
Number of reflections | 10666 | |
<I/σ(I)> | 8 | 5.4 |
Completeness [%] | 87.6 | 76.1 |
Redundancy | 7.8 | 5.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Batch method * | 8.1 | 293 | Wengler, G., (1999) Virology, 257, 472. * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | 1 | protein | 20 (mg/ml) | |
2 | 1 | 1 | PEG8000 | 1-5 (%(w/v)) |