5DSD
The crystal structure of the C-terminal domain of Ebola (Bundibugyo) nucleoprotein
Replaces: 5CIJExperimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 21-ID-D |
Synchrotron site | APS |
Beamline | 21-ID-D |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2014-08-14 |
Detector | RAYONIX MX300HE |
Wavelength(s) | 0.99 |
Spacegroup name | P 64 2 2 |
Unit cell lengths | 108.957, 108.957, 82.736 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 80.000 - 2.310 |
R-factor | 0.1692 |
Rwork | 0.168 |
R-free | 0.20250 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4qb0 |
RMSD bond length | 0.008 |
RMSD bond angle | 1.253 |
Data reduction software | HKL-3000 |
Data scaling software | SCALEPACK |
Phasing software | HKL-3000 |
Refinement software | REFMAC (5.8.0103) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 80.000 | 2.380 |
High resolution limit [Å] | 2.300 | 2.300 |
Rmerge | 0.084 | 0.432 |
Number of reflections | 12398 | |
<I/σ(I)> | 20.3 | 1.9 |
Completeness [%] | 94.3 | 64.7 |
Redundancy | 14.8 | 7.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 293 | Crystallization solution: 1.33 M LiSO4, 0.1 M Tris pH 8.5. 1:1 ratio (250 nL: 250 nL) of precipitant to protein (at a concentration of 13.9 mg/ml). 60 mcL reservoir. Protein purification buffer 50mM Tris-HCl, 150 mM NaCl; pH 7.5 |