1RER
Crystal structure of the homotrimer of fusion glycoprotein E1 from Semliki Forest Virus.
Experimental procedure
Experimental method | MAD |
Source type | SYNCHROTRON |
Source details | SLS BEAMLINE X06SA |
Synchrotron site | SLS |
Beamline | X06SA |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2003-03-03 |
Detector | MARRESEARCH |
Wavelength(s) | 1.53596, 1.53646, 1.18080 |
Spacegroup name | P 31 2 1 |
Unit cell lengths | 198.197, 198.197, 116.250 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 20.000 - 3.200 |
R-factor | 0.266 |
Rwork | 0.265 |
R-free | 0.28500 |
Structure solution method | MAD, MIR |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | SOLVE |
Refinement software | CNS |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 20.000 |
High resolution limit [Å] | 3.200 |
Number of reflections | 40912 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 4 | 4 * | PEG 400, NaBr, detergent DDAO, HO3+, VAPOR DIFFUSION, HANGING DROP |
1 | VAPOR DIFFUSION, HANGING DROP | 4 | 4 * | PEG 400, NaBr, detergent DDAO, HO3+, VAPOR DIFFUSION, HANGING DROP |
1 | VAPOR DIFFUSION, HANGING DROP | 4 | 4 * | PEG 400, NaBr, detergent DDAO, HO3+, VAPOR DIFFUSION, HANGING DROP |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | reservoir | DDAO | 15 (mM) | |
2 | 1 | reservoir | 250 (mM) | ||
3 | 1 | reservoir | Tris-HCl | 25 (mM) | |
4 | 1 | reservoir | PEG4000 | 2.5-12.5 (%) | pH4. |