5NPO
Promiscuous Protein Self-Assembly as a Function of Protein Stability
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE MASSIF-3 |
Synchrotron site | ESRF |
Beamline | MASSIF-3 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2017-02-15 |
Detector | DECTRIS EIGER R 4M |
Wavelength(s) | 0.9677 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 66.909, 52.733, 67.944 |
Unit cell angles | 90.00, 90.59, 90.00 |
Refinement procedure
Resolution | 67.940 - 1.950 |
R-factor | 0.20168 |
Rwork | 0.199 |
R-free | 0.25582 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4op5 |
RMSD bond length | 0.018 |
RMSD bond angle | 1.913 |
Data reduction software | XDS |
Data scaling software | XDS |
Phasing software | PHASER |
Refinement software | REFMAC (5.8.0158) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 67.940 | 1.980 |
High resolution limit [Å] | 1.950 | 1.950 |
Number of reflections | 34416 | 1696 |
<I/σ(I)> | 12.9 | 2.2 |
Completeness [%] | 98.9 | 99.8 |
Redundancy | 5.9 | 6.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5.5 | 292 | 7.5% PEG 6000, 0.1M MgCl2 and 0.05M Sodium acetate pH=5.5 |