4RHZ
Crystal structure of Cry23Aa1 and Cry37Aa1 binary protein complex
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 17-ID |
| Synchrotron site | APS |
| Beamline | 17-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2000-03-15 |
| Detector | MARRESEARCH |
| Wavelength(s) | 1.00 |
| Spacegroup name | P 61 |
| Unit cell lengths | 126.390, 126.390, 79.234 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 49.500 - 2.350 |
| R-factor | 0.19474 |
| Rwork | 0.192 |
| R-free | 0.24549 |
| Structure solution method | MIR |
| RMSD bond length | 0.024 |
| RMSD bond angle | 2.069 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | SOLVE |
| Refinement software | REFMAC (5.5.0102) |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 109.000 |
| High resolution limit [Å] | 2.350 |
| Rmerge | 0.050 |
| Number of reflections | 30216 |
| <I/σ(I)> | 49.1 |
| Completeness [%] | 99.9 |
| Redundancy | 10.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 296 | The protein sample was at a concentration of 2.1mg/mL in 25mM ethanolamine, and was prepared from chromatography fractions containing the co-eluted protein complex. For vapor diffusion crystallization, the precipitant solution was 2-6%(w/v) PEG8000 in 0.1M Tris-pH 8.5 buffer. A droplet using 2uL of protein and 2uL of precipitant solution was placed over a well containing 500 uL of precipitant solution. Crystals appeared within one week., VAPOR DIFFUSION, HANGING DROP, temperature 296K |
