5DU1
Crystal structure of Dendroaspis polylepis mambalgin-1 wild-type in P21 space group.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE MASSIF-1 |
| Synchrotron site | ESRF |
| Beamline | MASSIF-1 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2015-01-29 |
| Detector | DECTRIS PILATUS 2M |
| Wavelength(s) | 0.965 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 39.030, 50.240, 46.880 |
| Unit cell angles | 90.00, 93.38, 90.00 |
Refinement procedure
| Resolution | 38.960 - 1.800 |
| R-factor | 0.17662 |
| Rwork | 0.174 |
| R-free | 0.22433 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5do6 |
| RMSD bond length | 0.019 |
| RMSD bond angle | 2.065 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.8.0123) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 46.796 | 1.910 |
| High resolution limit [Å] | 1.800 | 1.800 |
| Rmerge | 0.063 | 0.257 |
| Number of reflections | 15969 | |
| <I/σ(I)> | 13.77 | 4.35 |
| Completeness [%] | 93.8 | 84.7 |
| Redundancy | 2.7 | 2.77 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6 | 293 | protein: 5 mg/mL in 0.550 M Na Acetate pH 5.5 precipitant: 18% PEG4K, 3% MPD, 3% 1,4-dioxane, .188 M Imidazole Malate, pH 6 cryoprotectant:: CrySol-SM5, 30% PEG 600, 0.1 M mixed (Na acetate, ADA, Bicine), pH 7.5 |
