1N64
Crystal structure analysis of the immunodominant antigenic site on Hepatitis C virus protein bound to mAb 19D9D6
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE BM30A |
Synchrotron site | ESRF |
Beamline | BM30A |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2001-03-30 |
Detector | MARRESEARCH |
Wavelength(s) | 1.009112 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 42.180, 101.700, 55.180 |
Unit cell angles | 90.00, 98.70, 90.00 |
Refinement procedure
Resolution | 20.000 - 2.340 |
R-factor | 0.268 |
Rwork | 0.190 |
R-free | 0.24500 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | PDB ENTRIES 1UCB; 1DBA; 1HIL |
RMSD bond length | 0.006 |
RMSD bond angle | 1.400 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 2.390 |
High resolution limit [Å] | 2.340 | 2.340 |
Rmerge | 0.067 * | 0.233 * |
Total number of observations | 17893 * | |
Number of reflections | 14779 * | |
<I/σ(I)> | 9.2 | 1.5 |
Completeness [%] | 98.8 * | 91.3 |
Redundancy | 3 | 1.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | unknown * | 9 | 291 | Stura, E.A., (2001) J. Crystal Growth, 232, 545. * |