7SVP
Structure of compound 34 bound to human Phospholipase D2 catalytic domain
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SLS BEAMLINE X06SA |
| Synchrotron site | SLS |
| Beamline | X06SA |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2020-09-20 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 0.97 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 89.721, 132.238, 113.861 |
| Unit cell angles | 90.00, 100.65, 90.00 |
Refinement procedure
| Resolution | 111.000 - 2.900 |
| R-factor | 0.2918 |
| Rwork | 0.290 |
| R-free | 0.32660 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 6oho |
| RMSD bond length | 0.002 |
| RMSD bond angle | 0.469 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | PHENIX |
| Refinement software | PHENIX (1.19.2_4158) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 111.000 | 3.140 |
| High resolution limit [Å] | 2.900 | 3.050 |
| Rmerge | 0.280 | |
| Number of reflections | 57790 | 2260 |
| <I/σ(I)> | 3.82 | |
| Completeness [%] | 99.0 | |
| Redundancy | 3.5 | |
| CC(1/2) | 0.990 | 0.445 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.6 | 291 | 0.08 M sodium cacodylate pH 6.6, 14% PEG 8000, 20% glycerol, 0.16 M calcium acetate |
