5FLR
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 | 42.395, 41.628, 72.267 |
| Unit cell angles | 90.00, 104.61, 90.00 |
Refinement procedure
| Resolution | 69.930 - 1.680 |
| R-factor | 0.14938 |
| Rwork | 0.147 |
| R-free | 0.20460 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4cq0 |
| RMSD bond length | 0.019 |
| RMSD bond angle | 1.930 |
| 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] | 41.600 | 1.710 |
| High resolution limit [Å] | 1.680 | 1.680 |
| Rmerge | 0.120 | 0.700 |
| Number of reflections | 27965 | |
| <I/σ(I)> | 11.1 | 2.3 |
| Completeness [%] | 99.2 | 85.4 |
| Redundancy | 7.3 | 6.4 |
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. |
