2Y57
Fragment growing induces conformational changes in acetylcholine- binding protein: A structural and thermodynamic analysis - (Compound 4)
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 | 2010-04-24 |
Detector | DECTRIS PILATUS 6M |
Spacegroup name | I 2 3 |
Unit cell lengths | 210.740, 210.740, 210.740 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 49.670 - 3.300 |
R-factor | 0.1637 |
Rwork | 0.162 |
R-free | 0.19340 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2c9t |
RMSD bond length | 0.010 |
RMSD bond angle | 1.150 |
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] | 14.740 | 3.380 |
High resolution limit [Å] | 3.300 | 3.300 |
Rmerge | 0.170 | 0.850 |
Number of reflections | 23584 | |
<I/σ(I)> | 11.6 | 1.81 |
Completeness [%] | 99.4 | 95.3 |
Redundancy | 5.07 | 4.97 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 8 | 0.1M MMT PH8.0, 1.3M AMMONIUM SULPHATE |