5YAX
Crystal structure of a human neutralizing antibody bound to a HBV preS1 peptide
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRF BEAMLINE BL17U1 |
Synchrotron site | SSRF |
Beamline | BL17U1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2013-07-26 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 0.9793 |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 142.670, 55.662, 67.696 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 19.923 - 2.500 |
R-factor | 0.2448 |
Rwork | 0.242 |
R-free | 0.28790 |
RMSD bond length | 0.002 |
RMSD bond angle | 0.572 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | PHASER |
Refinement software | PHENIX (1.9_1692) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 2.540 |
High resolution limit [Å] | 2.500 | 2.500 |
Rmerge | 0.144 | 0.321 |
Number of reflections | 19392 | 886 |
<I/σ(I)> | 17.7 | 6.2 |
Completeness [%] | 96.0 | 94.9 |
Redundancy | 5.8 | 5.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 293 | sodium acetate |