4BFQ
Assembly of a triple pi-stack of ligands in the binding site of Aplysia californica acetylcholine binding protein (AChBP)
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 | 2010-03-20 |
| Detector | DECTRIS PILATUS 6M |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 80.730, 78.330, 106.530 |
| Unit cell angles | 90.00, 102.67, 90.00 |
Refinement procedure
| Resolution | 41.260 - 2.400 |
| R-factor | 0.21156 |
| Rwork | 0.210 |
| R-free | 0.24724 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2W8E |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.315 |
| Data reduction software | iMOSFLM |
| Data scaling software | SCALA |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.7.0005) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 43.300 | 2.530 |
| High resolution limit [Å] | 2.400 | 2.400 |
| Rmerge | 0.130 | 0.760 |
| Number of reflections | 47324 | |
| <I/σ(I)> | 5.9 | 1.8 |
| Completeness [%] | 93.0 | 92.6 |
| Redundancy | 2.4 | 2.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION | 8 | 292 | THE VUF9432-AC-ACHBP COMPLEX WAS FORMED BY MIXING THE PROTEIN AT 3.5 MG/ML WITH 1MM VUF9432 AND INCUBATING ON ICE FOR 1 HOUR. CRYSTALS WERE GROWN USING THE VAPOUR DIFFUSION METHOD IN A SOLUTION CONSISTING OF 0.2M LISO4, 0.8M AMMONIUM SULPHATE IN MMT BUFFER (PH 8.0) AND 19 DEGREES C |
