6B6Z
Crystal structure of the Apo Antibody fragment (Fab) raised against C-terminal domain of Ebola nucleoprotein (EBOV, TAFV, BDBV strains)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-BM |
| Synchrotron site | APS |
| Beamline | 19-BM |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2016-02-25 |
| Detector | ADSC QUANTUM 210r |
| Wavelength(s) | 1.000 |
| Spacegroup name | P 41 2 2 |
| Unit cell lengths | 74.621, 74.621, 323.695 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 19.974 - 2.112 |
| R-factor | 0.2053 |
| Rwork | 0.203 |
| R-free | 0.25760 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5vkd |
| RMSD bond length | 0.004 |
| RMSD bond angle | 0.800 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | PHENIX |
| Refinement software | PHENIX (1.9_1692) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 47.400 | 2.150 |
| High resolution limit [Å] | 2.110 | 2.110 |
| Number of reflections | 50593 | 2442 |
| <I/σ(I)> | 4.23 | |
| Completeness [%] | 93.7 | |
| Redundancy | 6.2 | 5.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 288 | 180 mM Zinc Acetate, 90 mM imidazole, pH 8.0, 27% PEG 3000, 10 mM Chromium (III) chloride hexahydrate |
