5MZF
Crystal structure of dog MTH1 protein
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | BESSY BEAMLINE 14.1 |
| Synchrotron site | BESSY |
| Beamline | 14.1 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2014-12-07 |
| Detector | DECTRIS PILATUS 6M |
| Wavelength(s) | 0.91841 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 56.459, 67.353, 93.256 |
| Unit cell angles | 90.00, 90.28, 90.00 |
Refinement procedure
| Resolution | 48.400 - 2.000 |
| R-factor | 0.19203 |
| Rwork | 0.190 |
| R-free | 0.23380 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3zr1 |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.316 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0073) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 48.400 | 2.050 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.099 | 0.345 |
| Number of reflections | 47302 | |
| <I/σ(I)> | 9.5 | 3.7 |
| Completeness [%] | 99.6 | 99.8 |
| Redundancy | 3.8 | 3.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 293.15 | 0.1 M Sodium acetate, pH 3.5, 0.2 M Li2SO4, 0.5 % w/v n-octyl-beta-D-glucoside and 34 % PEG6000 |
