5WCF
Human HMT1 hnRNP methyltransferase-like protein 6 (S. cerevisiae)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | CLSI BEAMLINE 08ID-1 |
| Synchrotron site | CLSI |
| Beamline | 08ID-1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2015-05-17 |
| Detector | RAYONIX MX-300 |
| Wavelength(s) | 0.97949 |
| Spacegroup name | I 41 |
| Unit cell lengths | 94.721, 94.721, 108.713 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 50.000 - 1.980 |
| R-factor | 0.1999 |
| Rwork | 0.200 |
| R-free | 0.20820 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4hc4 |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.372 |
| Data reduction software | HKL-3000 |
| Data scaling software | SCALEPACK |
| Phasing software | HKL-3000 |
| Refinement software | REFMAC (5.8.0158) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 2.010 |
| High resolution limit [Å] | 1.980 | 5.370 | 1.980 |
| Rmerge | 0.060 | 0.033 | 0.907 |
| Rmeas | 0.065 | 0.035 | 0.973 |
| Rpim | 0.024 | 0.013 | 0.351 |
| Total number of observations | 253023 | ||
| Number of reflections | 33057 | 1649 | |
| <I/σ(I)> | 13 | ||
| Completeness [%] | 100.0 | 99.4 | 100 |
| Redundancy | 7.7 | 7.5 | 7.7 |
| CC(1/2) | 0.999 | 0.758 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 291 | 15% PEG 8000, 0.2M MgCl2, 0.1M Tris-HCl pH8.5 |
