Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 21-ID-G |
| Synchrotron site | APS |
| Beamline | 21-ID-G |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2014-02-23 |
| Detector | RAYONIX MX-300 |
| Wavelength(s) | 0.9786 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 50.367, 71.735, 142.913 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 29.140 - 2.700 |
| Rwork | 0.274 |
| R-free | 0.32480 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | trypsin activated Cry6Aa |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 50.000 |
| High resolution limit [Å] | 2.700 |
| Rmerge | 0.146 |
| Number of reflections | 14755 |
| <I/σ(I)> | 10.98 |
| Completeness [%] | 99.5 |
| Redundancy | 6.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 4.6 | 291 | Cry6Aa protein crystals were grown at 291 K from sitting drops containing the protein sample and reservoir solution (0.1 M citric acid, pH 4.6, 4% PEG 6,000). |
