1EA5
NATIVE ACETYLCHOLINESTERASE (E.C. 3.1.1.7) FROM TORPEDO CALIFORNICA at 1.8A resolution
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-4 |
| Synchrotron site | ESRF |
| Beamline | ID14-4 |
| Temperature [K] | 155 |
| Detector technology | CCD |
| Collection date | 1999-06-15 |
| Detector | ADSC CCD |
| Spacegroup name | P 31 2 1 |
| Unit cell lengths | 111.573, 111.573, 137.587 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 27.340 - 1.800 |
| R-factor | 0.185 |
| Rwork | 0.185 |
| R-free | 0.20500 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2ace |
| RMSD bond length | 0.016 |
| RMSD bond angle | 1.900 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | CNS |
| Refinement software | CNS (1.0) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 1.860 |
| High resolution limit [Å] | 1.800 | 1.800 |
| Number of reflections | 86444 | |
| <I/σ(I)> | 16.4 | 2.2 |
| Completeness [%] | 92.9 | 68.8 |
| Redundancy | 1.9 | 1.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 5.8 | 277 | PROTEIN WAS CRYSTALLIZED FROM 35% PEG 200, 100 MM MES, PH 5.8, AT 4 DEG. |
