2FY3
Structures of ligand bound human choline acetyltransferase provides insight into regulation of acetylcholine synthesis
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X8C |
| Synchrotron site | NSLS |
| Beamline | X8C |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2005-03-22 |
| Detector | ADSC QUANTUM 4 |
| Wavelength(s) | 1.1 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 54.780, 76.260, 164.290 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 17.900 - 2.270 |
| R-factor | 0.211 |
| Rwork | 0.196 |
| R-free | 0.23300 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1q6x |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.200 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | CNS (1.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 40.000 | 2.330 |
| High resolution limit [Å] | 2.250 | 2.250 |
| Rmerge | 0.065 | 0.198 |
| Number of reflections | 30580 | 1990 |
| <I/σ(I)> | 7 | |
| Completeness [%] | 90.6 | 60 |
| Redundancy | 5.8 | 5.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 277 | 11-13% PEG 3350, 0.1M Tris-HCl, 10mM acetylcholine, pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K |
