5FNI
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 | 42.687, 41.544, 72.090 |
| Unit cell angles | 90.00, 104.44, 90.00 |
Refinement procedure
| Resolution | 69.810 - 1.600 |
| R-factor | 0.15111 |
| Rwork | 0.149 |
| R-free | 0.19286 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4cq0 |
| RMSD bond length | 0.020 |
| RMSD bond angle | 1.944 |
| 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] | 41.500 | 1.630 |
| High resolution limit [Å] | 1.600 | 1.600 |
| Rmerge | 0.080 | 0.690 |
| Number of reflections | 31958 | |
| <I/σ(I)> | 16.7 | 2.3 |
| Completeness [%] | 97.9 | 75.8 |
| Redundancy | 7.2 | 5.4 |
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. |
