3GH3
Structural insights into the catalytic mechanism of CD38: Evidence for a conformationally flexible covalent enzyme-substrate complex.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 8.3.1 |
| Synchrotron site | ALS |
| Beamline | 8.3.1 |
| Temperature [K] | 77 |
| Detector technology | CCD |
| Collection date | 2006-06-10 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 1.11587 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 47.483, 80.879, 151.790 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 40.440 - 1.800 |
| R-factor | 0.1802 |
| Rwork | 0.177 |
| R-free | 0.22310 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3gc6 |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.124 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHENIX (PHASER) |
| Refinement software | PHENIX ((phenix.refine)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.860 |
| High resolution limit [Å] | 1.800 | 1.800 |
| Number of reflections | 53100 | |
| <I/σ(I)> | 26 | 2.91 |
| Completeness [%] | 96.6 | 89.3 |
| Redundancy | 3.9 | 3.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6 | 293 | 20-30% PEG 4000, 50-250MM AMMONIUM SULFATE, 100 MM SODIUM CACODYLATE OR SODIUM ACETATE OR MES AT PH-6.0-6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
