2V33
High resolution crystal structure of domain III of E1 fusion glycoprotein of Semliki Forest Virus
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-2 |
Synchrotron site | ESRF |
Beamline | ID14-2 |
Temperature [K] | 120 |
Detector technology | CCD |
Collection date | 2005-11-04 |
Detector | ADSC CCD |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 60.343, 62.659, 113.735 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 28.570 - 1.550 |
R-factor | 0.199 |
Rwork | 0.198 |
R-free | 0.22600 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1RER (DOMAIN III) |
RMSD bond length | 0.010 |
RMSD bond angle | 1.369 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 28.570 | 1.550 |
High resolution limit [Å] | 1.550 | 1.500 |
Rmerge | 0.050 | 0.560 |
Number of reflections | 31583 | |
<I/σ(I)> | 23.7 | |
Completeness [%] | 98.8 | 95.9 |
Redundancy | 4.4 | 3.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 25% PEG 8K, 0.2M NA ACETATE, 0.1M CACO PH 6.5, VAPOR DIFFUSION, HANGING DROP |