5E2X
The crystal structure of the C-terminal domain of Ebola (Tai Forest) nucleoprotein
Replaces: 5CIIExperimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-ID |
| Synchrotron site | APS |
| Beamline | 19-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2014-11-06 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.979 |
| Spacegroup name | P 1 |
| Unit cell lengths | 57.847, 60.075, 73.547 |
| Unit cell angles | 69.15, 68.93, 89.93 |
Refinement procedure
| Resolution | 50.000 - 2.100 |
| R-factor | 0.1946 |
| Rwork | 0.191 |
| R-free | 0.25970 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4qb0 |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.092 |
| Data reduction software | HKL-3000 |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.8.0124) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 2.140 |
| High resolution limit [Å] | 2.100 | 5.700 | 2.100 |
| Rmerge | 0.070 | 0.038 | 0.316 |
| Rmeas | 0.096 | 0.052 | 0.436 |
| Rpim | 0.065 | 0.035 | 0.299 |
| Total number of observations | 103077 | ||
| Number of reflections | 48426 | ||
| <I/σ(I)> | 7.8 | ||
| Completeness [%] | 96.1 | 97.1 | 84.6 |
| Redundancy | 2.1 | 2.2 | 2 |
| CC(1/2) | 0.995 | 0.789 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8.64 | 293 | Crystallization conditions: 10% PEG 3350, 0.1 M Tris-HCl/HEPES pH 8.64. 1:1 ratio of precipitant solution to protein, with a protein concentration of 5.0 mg/mL. There was a 1.5 M NaCl alternative reservoir |
