4YPI
Structure of Ebola virus nucleoprotein N-terminal fragment bound to a peptide derived from Ebola VP35
Experimental 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 | 2014-03-26 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 0.990 |
Spacegroup name | F 2 2 2 |
Unit cell lengths | 149.752, 194.818, 347.684 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 25.000 - 3.710 |
R-factor | 0.2546 |
Rwork | 0.253 |
R-free | 0.28500 |
Structure solution method | SAD |
RMSD bond length | 0.006 |
RMSD bond angle | 1.012 |
Data reduction software | HKL-3000 |
Data scaling software | HKL-2000 |
Phasing software | HKL-3000 |
Refinement software | REFMAC (5.8.0049) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 25.000 | 3.720 |
High resolution limit [Å] | 3.700 | 3.700 |
Rmerge | 0.115 | 0.242 |
Number of reflections | 23161 | |
<I/σ(I)> | 6.8 | 2 |
Completeness [%] | 84.7 | 10.2 |
Redundancy | 4.3 | 1.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 293 | streak seeding in well solution containing 100 mM Tris pH 7.2, 50 mM Hepes pH 7, and 23% PEG400 |