2BR7
Crystal Structure of Acetylcholine-binding Protein (AChBP) from Aplysia californica in complex with HEPES
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-2 |
Synchrotron site | ESRF |
Beamline | ID14-2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2004-09-30 |
Detector | ADSC CCD |
Spacegroup name | I 2 3 |
Unit cell lengths | 204.203, 204.203, 204.203 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 19.840 - 3.000 |
R-factor | 0.178 |
Rwork | 0.174 |
R-free | 0.24900 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1ux2 |
RMSD bond length | 0.012 |
RMSD bond angle | 1.506 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | AMoRE |
Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 3.160 |
High resolution limit [Å] | 3.000 | 3.000 |
Rmerge | 0.160 | 0.490 |
Number of reflections | 28431 | |
<I/σ(I)> | 4.5 | 1.5 |
Completeness [%] | 100.0 | 100 |
Redundancy | 8.1 | 8.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 7 | 100 MM HEPES 1.15 M SODIUM MALONATE, pH 7.00 |