6NEH
N191D, F205S mutant of scoulerine 9-O-methyltransferase from Thalictrum flavum complexed with (13aS)-3,10-dimethoxy-5,8,13,13a-tetrahydro-6H-isoquino[3,2-a]isoquinoline-2,9-diol and S-ADENOSYL-L-HOMOCYSTEINE
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRL BEAMLINE BL14-1 |
Synchrotron site | SSRL |
Beamline | BL14-1 |
Temperature [K] | 104 |
Detector technology | PIXEL |
Collection date | 2017-12-15 |
Detector | DECTRIS EIGER X 16M |
Wavelength(s) | 1.180763 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 61.130, 77.740, 67.350 |
Unit cell angles | 90.00, 91.85, 90.00 |
Refinement procedure
Resolution | 61.098 - 1.520 |
R-factor | 0.1571 |
Rwork | 0.156 |
R-free | 0.18180 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | Thalictrum Flavum Scoulerine 9-O-Methyltransferase N191D F205S |
RMSD bond length | 0.008 |
RMSD bond angle | 1.145 |
Data reduction software | iMOSFLM |
Data scaling software | Aimless |
Phasing software | PHASER |
Refinement software | PHENIX ((1.14_3260: ???)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 77.740 | 1.550 |
High resolution limit [Å] | 1.520 | 1.520 |
Rmerge | 0.056 | 0.449 |
Rmeas | 0.066 | 0.527 |
Rpim | 0.033 | 0.269 |
Number of reflections | 93910 | 4697 |
<I/σ(I)> | 12 | 2.5 |
Completeness [%] | 97.2 | 98.9 |
Redundancy | 3.7 | 3.7 |
CC(1/2) | 0.998 | 0.820 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 273 | 18% PEG 3,350 and 0.22M AMSO4 |