5CSD
Ligand binding domain 2 of Penicillium marneffei MP1 protein in complex with 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 | 58.502, 100.052, 99.050 |
| Unit cell angles | 90.00, 90.01, 90.00 |
Refinement procedure
| Resolution | 44.990 - 1.450 |
| R-factor | 0.1823 |
| Rwork | 0.181 |
| R-free | 0.20390 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.013 |
| RMSD bond angle | 1.673 |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER (2.2.1) |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 1.500 |
| High resolution limit [Å] | 1.450 | 3.120 | 1.450 |
| Rmerge | 0.087 | 0.074 | 0.303 |
| Total number of observations | 393148 | ||
| Number of reflections | 100087 | ||
| <I/σ(I)> | 13.8 | ||
| Completeness [%] | 99.2 | 98.5 | 95.8 |
| Redundancy | 3.9 | 4 | 3.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 4.8 | 298 | PEG 4000, Sodium Acetate, Ammonium Acetate |
