4HC4
Human HMT1 hnRNP methyltransferase-like protein 6 (S. cerevisiae)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-ID |
| Synchrotron site | APS |
| Beamline | 19-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2012-08-16 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.97934 |
| Spacegroup name | I 41 |
| Unit cell lengths | 93.981, 93.981, 108.878 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 33.250 - 1.970 |
| R-factor | 0.18918 |
| Rwork | 0.188 |
| R-free | 0.22017 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1g6q |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.173 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | PHASER (2.1.4) |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.000 |
| High resolution limit [Å] | 1.970 | 1.970 |
| Number of reflections | 33354 | |
| <I/σ(I)> | 42.1 | 2.8 |
| Completeness [%] | 99.9 | 100 |
| Redundancy | 10 | 10 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7 | 293 | Purified HRMT1L6 was complexed with SAH at 1:5 molar ratio of protein:SAH and crystallized by mixing 1 ul of the protein solution with 1 ul of the reservoir solution containing 15% PEG3350, 0.1 M succinate acid, pH 7.0, vapor diffusion, hanging drop, temperature 293K |
