5FB7
Ligand binding domain 2 of Penicillium marneffei MP1 protein complexed with multiple arachidonic acids
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRF BEAMLINE BL17U |
| Synchrotron site | SSRF |
| Beamline | BL17U |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2012-03-26 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.9793 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 59.239, 98.495, 100.120 |
| Unit cell angles | 90.00, 90.01, 90.00 |
Refinement procedure
| Resolution | 50.000 - 1.500 |
| R-factor | 0.1923 |
| Rwork | 0.191 |
| R-free | 0.21690 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5csd |
| RMSD bond length | 0.017 |
| RMSD bond angle | 1.432 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 1.550 |
| High resolution limit [Å] | 1.500 | 3.230 | 1.500 |
| Rmerge | 0.066 | 0.045 | 0.567 |
| Total number of observations | 668581 | ||
| Number of reflections | 90586 | ||
| <I/σ(I)> | 13 | ||
| Completeness [%] | 98.9 | 90.2 | 100 |
| Redundancy | 7.4 | 6.9 | 7.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 4.6 | 298 | PEG 4000, sodium acetate, ammonium acetate |
