3X0L
ADP ribose pyrophosphatase from Thermus thermophilus HB8 in ES-state at 1.00 angstrom resolution
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SPRING-8 BEAMLINE BL38B1 |
Synchrotron site | SPring-8 |
Beamline | BL38B1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2010-12-14 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 0.7 |
Spacegroup name | P 32 2 1 |
Unit cell lengths | 49.576, 49.576, 119.399 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 20.000 - 1.000 |
R-factor | 0.139 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3x0i |
RMSD bond length | 0.019 |
RMSD bond angle | 2.660 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | MOLREP |
Refinement software | SHELXL-97 |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 20.000 | 20.000 | 1.020 |
High resolution limit [Å] | 1.000 | 2.710 | 1.000 |
Number of reflections | 90869 | ||
Completeness [%] | 97.9 | 94.8 | 96.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 4.6 | 298 | 0.24M Acetate-Sodium acetate buffer, 0.32M Ammonium sulfate, 30%(w/v) Glycerol, 10%(w/v) PEG 20000, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 298K |