4M0F
Structure of human acetylcholinesterase in complex with territrem B
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X29A |
| Synchrotron site | NSLS |
| Beamline | X29A |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2013-03-21 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 1.075 |
| Spacegroup name | P 31 2 1 |
| Unit cell lengths | 105.143, 105.143, 322.281 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 41.087 - 2.304 |
| R-factor | 0.1769 |
| Rwork | 0.175 |
| R-free | 0.21130 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4ey4 |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.348 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.8.2_1309) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 2.340 |
| High resolution limit [Å] | 2.300 | 6.240 | 2.300 |
| Rmerge | 0.080 | 0.035 | 0.661 |
| Number of reflections | 91760 | ||
| <I/σ(I)> | 7.7 | ||
| Completeness [%] | 99.6 | 98.4 | 100 |
| Redundancy | 4.1 | 3.8 | 4.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7 | 295 | 12 to 18% PEG 3350, 0.2M potassium nitrate, pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 295K |
