5ECF
Ligand binding domain 1 of Penicillium marneffei MP1 protein complexed with arachidonic acids
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SOLEIL BEAMLINE PROXIMA 1 |
| Synchrotron site | SOLEIL |
| Beamline | PROXIMA 1 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2013-06-28 |
| Detector | DECTRIS PILATUS 6M |
| Wavelength(s) | 0.99187 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 65.675, 104.274, 108.103 |
| Unit cell angles | 90.00, 97.44, 90.00 |
Refinement procedure
| Resolution | 50.000 - 2.600 |
| R-factor | 0.2577 |
| Rwork | 0.256 |
| R-free | 0.29010 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5e7x |
| RMSD bond length | 0.017 |
| RMSD bond angle | 1.073 |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER (2.5.2) |
| Refinement software | REFMAC (5.8.0123) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 2.690 |
| High resolution limit [Å] | 2.600 | 5.601 | 2.600 |
| Rmerge | 0.074 | 0.050 | 0.390 |
| Total number of observations | 153960 | ||
| Number of reflections | 42305 | ||
| <I/σ(I)> | 8.7 | ||
| Completeness [%] | 94.4 | 98.9 | 69.7 |
| Redundancy | 3.6 | 3.8 | 2.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 4.6 | 298 | PEG 4000, sodium acetate, ammonium acetate |
