4AQD
Crystal structure of fully glycosylated human butyrylcholinesterase
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID23-1 |
| Synchrotron site | ESRF |
| Beamline | ID23-1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2011-05-08 |
| Detector | ADSC QUANTUM 315r |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 72.750, 79.260, 227.200 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 39.041 - 2.500 |
| R-factor | 0.1652 |
| Rwork | 0.163 |
| R-free | 0.23200 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1p0i |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.231 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | PHENIX (AUTOMR) |
| Refinement software | PHENIX ((PHENIX.REFINE)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 39.000 | 2.600 |
| High resolution limit [Å] | 2.500 | 2.500 |
| Rmerge | 0.060 | 0.640 |
| Number of reflections | 46071 | |
| <I/σ(I)> | 22.3 | 3.3 |
| Completeness [%] | 99.4 | 97.7 |
| Redundancy | 6.1 | 5.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 7.4 | 293 | PROTEIN WAS CRYSTALLIZED FROM 20% PEG 3350, 0.2 M NH4OAC PH 7.4, AT 293 K |
