1ES6
CRYSTAL STRUCTURE OF THE MATRIX PROTEIN OF EBOLA VIRUS
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE BM14 |
| Synchrotron site | ESRF |
| Beamline | BM14 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 1999-11-08 |
| Detector | MARRESEARCH |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 64.637, 91.094, 49.226 |
| Unit cell angles | 90.00, 97.35, 90.00 |
Refinement procedure
| Resolution | 25.000 - 2.000 |
| R-factor | 0.22 * |
| Rwork | 0.220 |
| R-free | 0.25000 |
| Structure solution method | MAD |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.470 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | SHARP |
| Refinement software | CNS (0.9) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 25.000 | 2.050 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.039 | 0.224 |
| Total number of observations | 166358 * | |
| Number of reflections | 17806 | |
| <I/σ(I)> | 10.6 | |
| Completeness [%] | 93.7 | 86.8 * |
| Redundancy | 8.7 | 3.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 298 | Dessen, A., (2000) Acta Crystallogr., Sect.D, 56, 758. * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | reservoir | Tris | 100 (mM) | |
| 2 | 1 | reservoir | PEG750 MME | 25 (%) | |
| 3 | 1 | reservoir | 100 (mM) | ||
| 4 | 1 | reservoir | beta-octylglucoside | 0.2 (%) |
