7SKU
Nipah virus matrix protein in complex with PI(4,5)P2
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 | PIXEL |
Collection date | 2019-08-09 |
Detector | DECTRIS EIGER X 16M |
Wavelength(s) | 1.03317 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 70.114, 96.471, 119.972 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 75.180 - 2.117 |
R-factor | 0.2327 |
Rwork | 0.231 |
R-free | 0.26420 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 7skt |
RMSD bond length | 0.008 |
RMSD bond angle | 0.990 |
Data reduction software | XDS (Feb 5, 2021) |
Data scaling software | Aimless (0.7.7) |
Phasing software | PHASER |
Refinement software | BUSTER (2.10.4) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 75.180 | 75.180 | 2.154 |
High resolution limit [Å] | 2.117 | 5.746 | 2.117 |
Rmerge | 0.201 | 0.047 | 3.308 |
Rmeas | 0.209 | 0.049 | 3.460 |
Rpim | 0.058 | 0.014 | 0.996 |
Total number of observations | 579838 | 29619 | 26354 |
Number of reflections | 45637 | 2544 | 2288 |
<I/σ(I)> | 9.95 | 35.79 | 0.72 |
Completeness [%] | 96.9 | 99.9 | 100 |
Redundancy | 12.71 | 11.64 | 11.52 |
CC(1/2) | 0.998 | 0.999 | 0.380 |
Anomalous redundancy | 6.7 | 6.7 | 6.0 |
CC(ano) | -0.076 | -0.126 | -0.005 |
|DANO|/σ(DANO) | 0.8 | 0.7 | 0.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 293 | 0.1 M HEPES pH 7.5, 2.0 M ammonium sulfate |