6P28
Crystal structure of the MIR domain (aa 337-532) of the S. cerevisiae mannosyltransferase Pmt2
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 21-ID-D |
| Synchrotron site | APS |
| Beamline | 21-ID-D |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2018-10-08 |
| Detector | DECTRIS EIGER X 9M |
| Wavelength(s) | 1.078 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 34.289, 71.403, 37.886 |
| Unit cell angles | 90.00, 96.37, 90.00 |
Refinement procedure
| Resolution | 37.650 - 1.350 |
| R-factor | 0.187 |
| Rwork | 0.187 |
| R-free | 0.21300 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 6p25 |
| RMSD bond length | 0.025 |
| RMSD bond angle | 2.359 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALA |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0155) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 37.650 | 1.380 |
| High resolution limit [Å] | 1.350 | 1.350 |
| Rmerge | 0.134 | 0.023 |
| Number of reflections | 40003 | 17096 |
| <I/σ(I)> | 13.4 | |
| Completeness [%] | 96.7 | |
| Redundancy | 3.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 293 | 25% PEG20000 MME |
