7XCL
Crystal structure of trimethylamine methyltransferase MttB from Methanosarcina barkeri at 2.5 A resolution
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSRRC BEAMLINE BL13B1 |
Synchrotron site | NSRRC |
Beamline | BL13B1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2019-04-10 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 0.99984 |
Spacegroup name | P 32 2 1 |
Unit cell lengths | 175.492, 175.492, 300.996 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 20.000 - 2.500 |
Rwork | 0.174 |
R-free | 0.21770 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2qne |
RMSD bond length | 0.007 |
RMSD bond angle | 1.256 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHASER |
Refinement software | CNS |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 20.000 | 20.000 | 2.540 |
High resolution limit [Å] | 2.500 | 6.700 | 2.500 |
Rmerge | 0.091 | 0.038 | 0.886 |
Rmeas | 0.100 | 0.041 | 0.982 |
Rpim | 0.040 | 0.015 | 0.409 |
Total number of observations | 932353 | ||
Number of reflections | 172408 | 9518 | 8376 |
<I/σ(I)> | 7 | ||
Completeness [%] | 93.8 | 98.9 | 92.1 |
Redundancy | 5.4 | 6.7 | 5 |
CC(1/2) | 0.998 | 0.747 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 283 | 1 ul protein (8 mg/mL MttB in 20 mM potassium phosphate buffer pH 7.4, 500 mM NaCl, 240 mM imidazole, 20% glycerol), 1 ul reservoir (4% MPD, 0.1 M citric acid pH 4.5) solutions |