5WT1
Pyrococcus abyssi methyltransferase PaTrm5a bound by SAH and cognate tRNA
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 | 2016-04-02 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 0.99 |
Spacegroup name | P 1 2 1 |
Unit cell lengths | 102.096, 57.017, 115.807 |
Unit cell angles | 90.00, 101.53, 90.00 |
Refinement procedure
Resolution | 40.217 - 2.598 |
R-factor | 0.2488 |
Rwork | 0.247 |
R-free | 0.27420 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2zzn |
RMSD bond length | 0.005 |
RMSD bond angle | 0.976 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHASER |
Refinement software | PHENIX ((1.10.1_2155)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.690 |
High resolution limit [Å] | 2.598 | 2.600 |
Rmerge | 0.077 | 0.911 |
Number of reflections | 40587 | |
<I/σ(I)> | 15.6 | 1.7 |
Completeness [%] | 99.5 | 99.9 |
Redundancy | 3.7 | 3.8 |
CC(1/2) | 0.739 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 298 | 45% MPD, 100 mM MES (pH 6.5), 200 mM NH4OAc |