4GAG
Structure of the broadly neutralizing antibody AP33 in complex with its HCV epitope (E2 residues 412-423)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU MICROMAX-007 HF |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2010-07-05 |
Detector | RIGAKU SATURN 944 |
Wavelength(s) | 1.5418 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 127.649, 56.903, 81.802 |
Unit cell angles | 90.00, 113.90, 90.00 |
Refinement procedure
Resolution | 23.110 - 1.800 |
R-factor | 0.17935 |
Rwork | 0.178 |
R-free | 0.21092 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.028 |
RMSD bond angle | 2.211 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHASER |
Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 50.000 |
High resolution limit [Å] | 1.800 |
Number of reflections | 49991 |
Completeness [%] | 98.3 |
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 |