5GM2
Crystal structure of methyltransferase TleD complexed with SAH and teleocidin A1
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRF BEAMLINE BL17U |
| Synchrotron site | SSRF |
| Beamline | BL17U |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2015-05-07 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.97915 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 257.459, 152.757, 154.171 |
| Unit cell angles | 90.00, 93.06, 90.00 |
Refinement procedure
| Resolution | 153.950 - 2.800 |
| R-factor | 0.2086 |
| Rwork | 0.207 |
| R-free | 0.24870 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.003 |
| RMSD bond angle | 0.713 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | PHENIX ((1.10.1_2155: ???)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 153.950 | 2.950 |
| High resolution limit [Å] | 2.800 | 2.800 |
| Rmerge | 0.072 | 0.484 |
| Number of reflections | 146088 | |
| <I/σ(I)> | 16.5 | 3.3 |
| Completeness [%] | 99.8 | 100 |
| Redundancy | 4.7 | 4.8 |
| CC(1/2) | 0.999 | 0.846 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8 | 291 | 100 mM Tris-HCl, 18% PEG400, 14% PEG3350, 100 mM MgCl2, 2mM TCEP |
