3BSF
Crystal Structure of the MTA/SAH nucleosidase
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | PHOTON FACTORY BEAMLINE AR-NW12A |
Synchrotron site | Photon Factory |
Beamline | AR-NW12A |
Temperature [K] | 95 |
Detector technology | CCD |
Collection date | 2007-06-23 |
Detector | ADSC QUANTUM 210 |
Wavelength(s) | 1.0000 |
Spacegroup name | P 31 2 1 |
Unit cell lengths | 79.349, 79.349, 138.152 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 50.000 - 2.900 |
R-factor | 0.2571 |
Rwork | 0.253 |
R-free | 0.29280 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.009 |
RMSD bond angle | 1.339 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | MOLREP |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 3.030 |
High resolution limit [Å] | 2.900 | 2.900 |
Number of reflections | 11186 | |
Completeness [%] | 96.5 | 100 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 295 | 0.1M Bis-Tris, 30% PEG MME 2000, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 295K |