4ZTI
Ebola virus nucleoprotein bound to VP35 chaperoning peptide P212121
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 23-ID-B |
Synchrotron site | APS |
Beamline | 23-ID-B |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2014-04-05 |
Detector | MARMOSAIC 300 mm CCD |
Wavelength(s) | 1.03318 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 94.881, 94.951, 112.106 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 48.270 - 2.400 |
R-factor | 0.1946 |
Rwork | 0.192 |
R-free | 0.24700 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4zta |
RMSD bond length | 0.014 |
RMSD bond angle | 1.482 |
Data reduction software | MOSFLM |
Data scaling software | Aimless (0.1.27) |
Phasing software | PHASER (2.5.7) |
Refinement software | REFMAC (5.8.0073) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 48.270 | 48.270 | 2.490 |
High resolution limit [Å] | 2.400 | 8.980 | 2.400 |
Rmerge | 0.151 | 0.091 | 1.556 |
Rpim | 0.060 | 0.039 | 0.607 |
Total number of observations | 298839 | 5566 | 31129 |
Number of reflections | 40325 | ||
<I/σ(I)> | 8.2 | 18.6 | 1.5 |
Completeness [%] | 100.0 | 99.3 | 99.8 |
Redundancy | 7.4 | 6.3 | 7.5 |
CC(1/2) | 0.993 | 0.989 | 0.575 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 4.4 | 277 | 2.0 M sodium formate, 100 mM sodium acetate pH 4.4 |