4GAJ
Structure of the broadly neutralizing antibody AP33 in complex with its HCV epitope (E2 residues 411-424)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU MICROMAX-007 HF |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2010-11-02 |
Detector | RIGAKU SATURN 944 |
Wavelength(s) | 1.5418 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 171.910, 40.670, 73.770 |
Unit cell angles | 90.00, 112.11, 90.00 |
Refinement procedure
Resolution | 20.000 - 2.510 |
R-factor | 0.24405 |
Rwork | 0.240 |
R-free | 0.31983 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.016 |
RMSD bond angle | 1.682 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | PHASER |
Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.640 |
High resolution limit [Å] | 2.500 | 2.500 |
Number of reflections | 16538 | |
Completeness [%] | 99.3 | 96.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 8 | 295 | 18% PEG 8K, 0.1M TrisHCl, 0.2M CaCl2, VAPOR DIFFUSION, SITTING DROP, temperature 295K |