8UY2
Methylenetetrahydrofolate reductase from Chaetomium thermophilum DSM 1495, AdoMet-bound, Inhibited (T) State
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 21-ID-D |
Synchrotron site | APS |
Beamline | 21-ID-D |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2022-03-31 |
Detector | DECTRIS EIGER X 9M |
Wavelength(s) | 1.1271 |
Spacegroup name | P 2 21 21 |
Unit cell lengths | 130.656, 149.948, 171.056 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 74.974 - 2.830 |
Rwork | 0.187 |
R-free | 0.20270 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.009 |
RMSD bond angle | 1.633 |
Data reduction software | DIALS |
Data scaling software | Aimless |
Phasing software | PHASER |
Refinement software | REFMAC (5.8.0419) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 75.087 | 74.970 | 2.890 |
High resolution limit [Å] | 2.830 | 14.430 | 2.830 |
Rmerge | 0.126 | 0.076 | 1.171 |
Rmeas | 0.149 | 0.091 | 1.383 |
Rpim | 0.077 | 0.048 | 0.724 |
Number of reflections | 80491 | 705 | 4556 |
<I/σ(I)> | 10.1 | ||
Completeness [%] | 99.8 | ||
Redundancy | 6.9 | 5.5 | 7.2 |
CC(1/2) | 0.987 | 0.972 | 0.672 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 4.8 | 293.15 | 1-1 protein to reservoir solution, Protein: 50 mg/mL, 50 mM potassium phosphate buffer (KPB), pH 7.4, containing 500 uM AoMet and 250 uM FAD Reservoir Solution: 0.1 M sodium acetate, pH 4.8, 0.2 M ammonium sulfate, 6% polyethylene glycol monomethyl ether 2,000 |