6F7Q
Human Butyrylcholinesterase complexed with N-Propargyliperidines
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE MASSIF-3 |
| Synchrotron site | ESRF |
| Beamline | MASSIF-3 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2015-11-06 |
| Detector | DECTRIS PILATUS3 2M |
| Wavelength(s) | 0.9679 |
| Spacegroup name | P 4 21 2 |
| Unit cell lengths | 152.140, 152.140, 141.910 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 49.109 - 2.600 |
| R-factor | 0.1944 |
| Rwork | 0.192 |
| R-free | 0.24810 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1POM |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.019 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | PHASER |
| Refinement software | PHENIX ((1.11.1_2575: ???)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 49.109 | 2.693 |
| High resolution limit [Å] | 2.600 | 2.600 |
| Rmerge | 0.097 | 0.961 |
| Number of reflections | 49669 | 4794 |
| <I/σ(I)> | 7.04 | |
| Completeness [%] | 94.0 | 94.78 |
| Redundancy | 2.8 | 2.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8.9 | 293 | 0.1 M Tris, 2.3 M ammonium sulfate |
