7SUC
XFEL Serial Crystallography Reveals the Room Temperature Structure of Methyl-Coenzyme M Reductase
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | FREE ELECTRON LASER |
Source details | SLAC LCLS BEAMLINE MFX |
Synchrotron site | SLAC LCLS |
Beamline | MFX |
Temperature [K] | 300 |
Detector technology | CCD |
Collection date | 2020-07-11 |
Detector | RAYONIX MX340-HS |
Wavelength(s) | 1.3007 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 83.082, 119.777, 123.210 |
Unit cell angles | 90.00, 91.73, 90.00 |
Refinement procedure
Resolution | 21.250 - 1.900 |
R-factor | 0.1528 |
Rwork | 0.152 |
R-free | 0.18630 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3m1v |
RMSD bond length | 0.004 |
RMSD bond angle | 0.817 |
Data reduction software | cctbx.xfel |
Data scaling software | cxi.merge |
Phasing software | PHASER |
Refinement software | PHENIX (1.20_4459) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 21.250 | 1.930 |
High resolution limit [Å] | 1.900 | 1.900 |
Number of reflections | 189345 | 9505 |
<I/σ(I)> | 3.356 | 0.696 |
Completeness [%] | 99.9 | 99.82 |
Redundancy | 41.43 | 9.89 |
CC(1/2) | 0.979 | 0.379 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.55 | 300 | 18% PEG 400, 150mM Mg Acetate, 100mM HEPES (pH 7.5) |