5MDM
Structural intermediates in the fusion associated transition of vesiculovirus glycoprotein
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID29 |
Synchrotron site | ESRF |
Beamline | ID29 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2011-11-16 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 0.978 |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 150.340, 228.210, 78.840 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 49.108 - 2.998 |
R-factor | 0.1895 |
Rwork | 0.188 |
R-free | 0.22220 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2CMZ |
RMSD bond length | 0.004 |
RMSD bond angle | 0.800 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | PHASER |
Refinement software | PHENIX (1.8.1_1168) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 3.100 |
High resolution limit [Å] | 2.998 | 2.998 |
Rmerge | 0.090 | 1.253 |
Number of reflections | 55165 | |
<I/σ(I)> | 16.7 | 1.5 |
Completeness [%] | 99.8 | 99 |
Redundancy | 6.7 | 6.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 293 | 14% PEG 3350, 0.3 M Na2SO4 and 0.1 M HEPES pH 7.6; final pH 7.5 |