9J01
Crystal Structure Sensory Appendage Protein 2 from Anopheles culicifacies
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE MASSIF-1 |
| Synchrotron site | ESRF |
| Beamline | MASSIF-1 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2023-12-21 |
| Detector | DECTRIS PILATUS3 2M |
| Wavelength(s) | 0.9654 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 31.365, 37.075, 41.014 |
| Unit cell angles | 90.00, 93.19, 90.00 |
Refinement procedure
| Resolution | 31.316 - 1.611 |
| R-factor | 0.1906 |
| Rwork | 0.188 |
| R-free | 0.23830 |
| Structure solution method | SAD |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.161 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | CRANK2 |
| Refinement software | PHENIX ((1.15rc1_3423: ???)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 37.080 | 1.670 |
| High resolution limit [Å] | 1.610 | 1.610 |
| Rmerge | 0.080 | 1.355 |
| Rmeas | 0.087 | 1.525 |
| Rpim | 0.034 | 0.680 |
| Total number of observations | 74827 | 4064 |
| Number of reflections | 12010 | 880 |
| <I/σ(I)> | 11.8 | 0.9 |
| Completeness [%] | 97.3 | |
| Redundancy | 6.2 | 4.6 |
| CC(1/2) | 0.999 | 0.576 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 4.5 | 293 | 0.1M Lithium chloride, 0.1M Sodium acetate pH 4.5, 36% v/v PEG 400, 0.05M Cadmium chloride |






