5FNJ
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 MX1 |
Synchrotron site | Australian Synchrotron |
Beamline | MX1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2015-04-08 |
Detector | ADSC CCD |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 42.514, 41.377, 72.337 |
Unit cell angles | 90.00, 104.46, 90.00 |
Refinement procedure
Resolution | 70.050 - 1.670 |
R-factor | 0.13982 |
Rwork | 0.138 |
R-free | 0.18286 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4cq0 |
RMSD bond length | 0.019 |
RMSD bond angle | 1.964 |
Data reduction software | XDS |
Data scaling software | Aimless |
Phasing software | PHASER |
Refinement software | REFMAC (5.8.0131) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 41.400 | 1.700 |
High resolution limit [Å] | 1.670 | 1.670 |
Rmerge | 0.070 | 0.470 |
Number of reflections | 28316 | |
<I/σ(I)> | 20.5 | 3.9 |
Completeness [%] | 99.0 | 95 |
Redundancy | 7.4 | 6.9 |
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. |