Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 21-ID-D |
| Synchrotron site | APS |
| Beamline | 21-ID-D |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2011-03-19 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 1.12675 |
| Spacegroup name | P 65 |
| Unit cell lengths | 112.967, 112.967, 76.627 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 30.010 - 2.000 |
| Rwork | 0.188 |
| R-free | 0.22800 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2nrj |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.070 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.061 | 0.229 |
| Number of reflections | 37186 | |
| <I/σ(I)> | 33.41 | |
| Completeness [%] | 98.8 | |
| Redundancy | 3.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 4.2 | 291 | Cry6Aa protein crystals were grown at 291 K from sitting drops containing the protein sample and reservoir solution (20% (w/v) PEG 1000, 0.1 M sodium phosphate dibasic/citric acid pH 4.2; 0.2 M lithium sulfate. |
