5CD1
Structure of an asymmetric tetramer of human tRNA m1A58 methyltransferase in a complex with SAH and tRNA3Lys
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 8.3.1 |
| Synchrotron site | ALS |
| Beamline | 8.3.1 |
| Temperature [K] | 103.15 |
| Detector technology | CCD |
| Collection date | 2014-09-05 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 1.11587 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 128.240, 137.440, 157.590 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 59.392 - 3.600 |
| R-factor | 0.2337 |
| Rwork | 0.232 |
| R-free | 0.27290 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5ccb |
| RMSD bond length | 0.004 |
| RMSD bond angle | 0.763 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.8.1_1168) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 102.300 | 3.690 |
| High resolution limit [Å] | 3.600 | 3.600 |
| Rmerge | 0.308 | 1.870 |
| Number of reflections | 32882 | |
| <I/σ(I)> | 6.4 | 1 |
| Completeness [%] | 99.3 | 99.8 |
| Redundancy | 4.3 | 4.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 289 | 1 microliter protein solution (4.8 mg/ml protein, 66.4 micromolar tRNA3Lys, 2mM SAH, 1mM MgCl2 and 50mM Hepes pH7.5) mixed with 1 microliter reservoir solution (0.1M NaAcetate, pH4.8-5.0,2% w/v PEG 4000, and 15% v/v MPD) over 1000 microliter reservoir solution |






