5H5E
The crystal structure of the yeast arginine methyltransferase SFM1 complexed with SAH
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 | 2016-07-13 |
Detector | ADSC QUANTUM 4 |
Wavelength(s) | 0.979 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 38.731, 58.035, 43.357 |
Unit cell angles | 90.00, 106.40, 90.00 |
Refinement procedure
Resolution | 37.155 - 2.090 |
R-factor | 0.1935 |
Rwork | 0.191 |
R-free | 0.24610 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5c77 |
RMSD bond length | 0.006 |
RMSD bond angle | 0.865 |
Data reduction software | HKL-3000 |
Data scaling software | HKL-3000 |
Phasing software | PHASER |
Refinement software | PHENIX ((1.10.1_2155)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.180 |
High resolution limit [Å] | 2.100 | 2.100 |
Rmerge | 0.089 | 0.496 |
Number of reflections | 10918 | |
<I/σ(I)> | 23.7 | 3.4 |
Completeness [%] | 99.7 | 99.5 |
Redundancy | 3.7 | 3.7 |
CC(1/2) | 0.840 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 298 | 0.2 M NaCl, 0.1 M Tris-HCl (pH 8.5), 38% PEG 3350 |