2Y54
Fragment growing induces conformational changes in acetylcholine- binding protein: A structural and thermodynamic analysis - (Fragment 1)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SLS BEAMLINE X06SA |
| Synchrotron site | SLS |
| Beamline | X06SA |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2010-02-05 |
| Detector | DECTRIS PILATUS 6M |
| Spacegroup name | I 2 3 |
| Unit cell lengths | 216.420, 216.420, 216.420 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 48.390 - 3.650 |
| R-factor | 0.1935 |
| Rwork | 0.192 |
| R-free | 0.21690 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2c9t |
| RMSD bond length | 0.008 |
| RMSD bond angle | 0.940 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | PHASER |
| Refinement software | BUSTER (2.8.0) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 16.330 | 3.750 |
| High resolution limit [Å] | 3.650 | 3.650 |
| Rmerge | 0.180 | 0.660 |
| Number of reflections | 18887 | |
| <I/σ(I)> | 10.19 | 2.78 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 5 | 4.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 7.5 | 0.1M MMT PH7.5, 0.9M AMMONIUM SULPHATE |
