1Z5P
Crystal structure of MTA/AdoHcy nucleosidase with a ligand-free purine binding site
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU300 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Detector | RIGAKU RAXIS IV |
Wavelength(s) | 1.5418 |
Spacegroup name | C 2 2 2 |
Unit cell lengths | 70.010, 127.520, 69.590 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 31.270 - 2.000 |
R-factor | 0.206 |
Rwork | 0.206 |
R-free | 0.23400 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1jys |
RMSD bond length | 0.011 |
RMSD bond angle | 1.700 |
Data reduction software | d*TREK |
Data scaling software | d*TREK |
Phasing software | CNS (1.1) |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 31.270 | 2.070 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.056 | 0.346 |
Number of reflections | 21178 | |
Completeness [%] | 97.4 | |
Redundancy | 9.8 | 9.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7 | 293 | ammonium sulfate, PEG 2000 MME, sodium HEPES, isopropanol, QX-10000024, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K |