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)) |
