2Y58
Fragment growing induces conformational changes in acetylcholine- binding protein: A structural and thermodynamic analysis - (Compound 6)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID23-2 |
| Synchrotron site | ESRF |
| Beamline | ID23-2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2010-08-29 |
| Detector | MARRESEARCH |
| Spacegroup name | I 2 3 |
| Unit cell lengths | 213.330, 213.330, 213.330 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 47.700 - 3.250 |
| R-factor | 0.1701 |
| Rwork | 0.169 |
| R-free | 0.19820 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2c9t |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.080 |
| 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] | 14.530 | 3.330 |
| High resolution limit [Å] | 3.250 | 3.250 |
| Rmerge | 0.180 | 0.740 |
| Number of reflections | 25505 | |
| <I/σ(I)> | 10.81 | 2.05 |
| Completeness [%] | 99.6 | 97.1 |
| Redundancy | 4.81 | 4.38 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 7 | 0.1M MMT PH 7.0, 1.4M AMMONIUM SULPHATE |
