2PGJ
Catalysis associated conformational changes revealed by human cd38 complexed with a non-hydrolyzable substrate analog
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | CHESS BEAMLINE A1 |
| Synchrotron site | CHESS |
| Beamline | A1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2006-09-23 |
| Detector | ADSC QUANTUM 210 |
| Wavelength(s) | 0.976 |
| Spacegroup name | P 1 |
| Unit cell lengths | 41.891, 53.195, 65.636 |
| Unit cell angles | 105.34, 91.96, 94.94 |
Refinement procedure
| Resolution | 28.410 - 1.710 |
| R-factor | 0.19239 |
| Rwork | 0.191 |
| R-free | 0.22359 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2o3t |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.182 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.3.0021) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 1.760 |
| High resolution limit [Å] | 1.700 | 1.700 |
| Rmerge | 0.082 | 0.318 |
| Number of reflections | 54368 | |
| <I/σ(I)> | 2.73 | |
| Completeness [%] | 92.7 | 71 |
| Redundancy | 3.6 | 2.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6 | 300 | 100 mM MES, pH 6.0, and 10% PEG 4000, VAPOR DIFFUSION, HANGING DROP, temperature 300K |
