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. * |
