5OAL
Crystal structure of mutant AChBP in complex with strychnine (T53F, Q74R, Y110A, I135S, G162E)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID23-1 |
Synchrotron site | ESRF |
Beamline | ID23-1 |
Temperature [K] | 150 |
Detector technology | CCD |
Collection date | 2015-12-12 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 0.97627 |
Spacegroup name | P 32 |
Unit cell lengths | 130.900, 130.900, 190.139 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 72.850 - 3.200 |
R-factor | 0.1898 |
Rwork | 0.188 |
R-free | 0.23053 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2xys |
RMSD bond length | 0.017 |
RMSD bond angle | 2.053 |
Data reduction software | XDS |
Data scaling software | Aimless |
Phasing software | PHASER |
Refinement software | REFMAC (5.8.0158) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 72.850 | 3.290 |
High resolution limit [Å] | 3.200 | 3.200 |
Rmerge | 0.212 | 1.073 |
Number of reflections | 59286 | 4605 |
<I/σ(I)> | 8.3 | 2.3 |
Completeness [%] | 98.7 | 98.5 |
Redundancy | 8.1 | 7.3 |
CC(1/2) | 0.991 | 0.691 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 293 | Reservoir buffer: 20 % PEG3350 0.2 M Mg formate Protein buffer: 50 mM trism 250 mM NaCl Ph 7.5, 0.5 mM strychnine |