2B25
Human putative tRNA(1-methyladenosine)methyltransferase
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | CHESS BEAMLINE F2 |
Synchrotron site | CHESS |
Beamline | F2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2005-05-09 |
Detector | ADSC QUANTUM 210 |
Wavelength(s) | 0.97914 |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 75.533, 157.106, 113.492 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 78.567 - 2.500 |
Rwork | 0.247 |
R-free | 0.28220 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1i9g |
RMSD bond length | 0.017 |
RMSD bond angle | 1.366 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | MOLREP |
Refinement software | REFMAC (refmac_5.2.0005) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 78.570 | 40.000 | 2.380 |
High resolution limit [Å] | 2.300 | 4.950 | 2.300 |
Rmerge | 0.082 | 0.064 | |
Number of reflections | 30305 | ||
Completeness [%] | 99.6 | ||
Redundancy | 5.7 | 5.2 | 5.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 293 | 11 % PEG3350, 0.2M lithium citrate, 0.1M BisTris, 10% PEG400, pH 6.5, vapor diffusion, hanging drop, temperature 293K |