2FY4
Structures of ligand bound human choline acetyltransferase provide insight into regulation of acetylcholine synthesis
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU RUH3R |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2005-07-14 |
| Detector | MARRESEARCH |
| Wavelength(s) | 1.5418 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 54.700, 73.980, 165.700 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 17.900 - 2.300 |
| R-factor | 0.219 |
| Rwork | 0.203 |
| R-free | 0.24000 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1q6x |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.300 |
| 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 | 2.380 |
| High resolution limit [Å] | 2.300 | 2.300 |
| Rmerge | 0.080 | 0.288 |
| Number of reflections | 30693 | 3026 |
| <I/σ(I)> | 6.7 | |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 11.7 | 11.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 277 | 11-13% PEG 3350, 0.1M Tris-HCl, crystal soaked in mother liquor and 20mM coenzyme A, pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K |
