1YMH
anti-HCV Fab 19D9D6 complexed with protein L (PpL) mutant A66W
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID29 |
| Synchrotron site | ESRF |
| Beamline | ID29 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2004-02-05 |
| Detector | ADSC QUANTUM 210 |
| Wavelength(s) | 0.720169 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 77.143, 111.469, 148.698 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 87.710 - 2.600 |
| R-factor | 0.2284 |
| Rwork | 0.224 |
| R-free | 0.30228 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1mhh |
| RMSD bond length | 0.065 |
| RMSD bond angle | 4.344 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.1.24) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 88.000 | 2.660 |
| High resolution limit [Å] | 2.600 | 2.600 |
| Rmerge | 0.058 | 0.489 |
| Number of reflections | 39109 | |
| <I/σ(I)> | 15 | 4 |
| Completeness [%] | 97.8 | 100 |
| Redundancy | 11 | 11 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 5.1 | 293 | 9% PEG5K, 100mM Na cacodylate, pH 5.1, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
