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)) |
