4WEN
Co-complex structure of the F4 fimbrial adhesin FaeG variant ac with llama single domain antibody V2
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SOLEIL BEAMLINE PROXIMA 1 |
Synchrotron site | SOLEIL |
Beamline | PROXIMA 1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2013-07-03 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 0.98 |
Spacegroup name | P 3 2 1 |
Unit cell lengths | 145.833, 145.833, 37.875 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 47.740 - 1.890 |
R-factor | 0.19016 |
Rwork | 0.188 |
R-free | 0.22599 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3hlr |
RMSD bond length | 0.020 |
RMSD bond angle | 2.106 |
Data reduction software | XDS |
Data scaling software | SCALA |
Phasing software | PHASER |
Refinement software | REFMAC (5.8.0049) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 47.740 | 2.000 |
High resolution limit [Å] | 1.890 | 1.890 |
Number of reflections | 36784 | |
<I/σ(I)> | 14.3 | 1.4 |
Completeness [%] | 99.7 | 97.7 |
Redundancy | 20.2 | 19.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 4.6 | 293 | 100 mM Sodium Acetate pH 4.6, 200 mM ammonium sulfate, 25 % w/v PEG 4000 |