1G9Q
COMPLEX STRUCTURE OF THE ADPR-ASE AND ITS SUBSTRATE ADP-RIBOSE
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSLS BEAMLINE X25 |
Synchrotron site | NSLS |
Beamline | X25 |
Detector technology | IMAGE PLATE |
Collection date | 1998-07-01 |
Detector | MARRESEARCH |
Wavelength(s) | 1.0 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 66.930, 67.890, 98.070 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 34.180 - 2.300 |
R-factor | 0.195 |
Rwork | 0.195 |
R-free | 0.25500 |
Structure solution method | MIRAS |
RMSD bond length | 0.014 |
RMSD bond angle | 1.600 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | SOLVE |
Refinement software | CNS (0.9) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 34.180 | |
High resolution limit [Å] | 2.000 | |
Rmerge | 0.140 | 0.220 * |
Total number of observations | 242509 * | |
Number of reflections | 30010 | |
Completeness [%] | 93.2 | 79.7 * |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 * | 18 * | drop contains protein and reservoir solution in a 2:1 ratio * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 20 (mg/ml) | |
2 | 1 | drop | Tris-Cl | 50 (mM) | |
3 | 1 | drop | EDTA | 1 (mM) | |
4 | 1 | reservoir | PEG8000 | 10 (%(w/v)) | |
5 | 1 | reservoir | PEG1000 | 10 (%(w/v)) |