2CX8
Crystal structure of methyltransferase with ligand(SAH)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SPRING-8 BEAMLINE BL26B2 |
Synchrotron site | SPring-8 |
Beamline | BL26B2 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2004-02-18 |
Detector | RIGAKU |
Wavelength(s) | 1.00 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 53.866, 77.821, 55.085 |
Unit cell angles | 90.00, 115.12, 90.00 |
Refinement procedure
Resolution | 48.770 - 2.530 |
R-factor | 0.223 |
Rwork | 0.223 |
R-free | 0.28500 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.007 |
RMSD bond angle | 1.400 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | MOLREP |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.620 |
High resolution limit [Å] | 2.530 | 2.530 |
Number of reflections | 13895 | |
<I/σ(I)> | 44.7 | |
Completeness [%] | 99.2 | 94.8 |
Redundancy | 4.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 293 | 25% PEG3350, 0.2M potassium formate, 1mM SAH, VAPOR DIFFUSION, HANGING DROP, temperature 293K |