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 |