5FNG
Native state mass spectrometry, surface plasmon resonance and X-ray crystallography correlate strongly as a fragment screening combination
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | AUSTRALIAN SYNCHROTRON BEAMLINE MX2 |
Synchrotron site | Australian Synchrotron |
Beamline | MX2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2015-04-28 |
Detector | ADSC CCD |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 42.345, 41.200, 71.706 |
Unit cell angles | 90.00, 104.52, 90.00 |
Refinement procedure
Resolution | 69.420 - 2.050 |
R-factor | 0.17843 |
Rwork | 0.176 |
R-free | 0.22918 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4cq0 |
RMSD bond length | 0.017 |
RMSD bond angle | 1.711 |
Data reduction software | XDS |
Data scaling software | Aimless |
Phasing software | PHASER |
Refinement software | REFMAC (5.8.0135) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 41.200 | 2.110 |
High resolution limit [Å] | 2.050 | 2.050 |
Rmerge | 0.210 | 0.780 |
Number of reflections | 15256 | |
<I/σ(I)> | 7.1 | 2.7 |
Completeness [%] | 100.0 | 100 |
Redundancy | 7 | 7.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 15 MG/ML PROTEIN WITH 2.7 M AMMONIUM SULFATE, 100 MM TRIS PH 8.5 AT 8 C IN SITTING DROPS. |