5VYF
Structure of single chain Fel d 1 bound to a neutralizing antibody
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 5.0.2 |
Synchrotron site | ALS |
Beamline | 5.0.2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2015-10-16 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 1.00 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 74.985, 131.480, 148.357 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 98.400 - 2.900 |
R-factor | 0.22711 |
Rwork | 0.225 |
R-free | 0.25942 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1puo 2r8s |
RMSD bond length | 0.007 |
RMSD bond angle | 1.174 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHASER |
Refinement software | REFMAC (5.8.0135) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 98.400 | 2.950 |
High resolution limit [Å] | 2.900 | 2.900 |
Rmerge | 0.132 | 1.000 |
Rpim | 0.055 | 0.446 |
Number of reflections | 33144 | 1596 |
<I/σ(I)> | 14.9 | 1.6 |
Completeness [%] | 99.9 | 99.8 |
Redundancy | 7.2 | 6.9 |
CC(1/2) | 0.753 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 298 | calcium acetate, sodium cacodylate, PEG 300 |