9IW5
Crystal Structure Sensory Appendage Proteins 2 from Anopheles culicifacies in space group P212121
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 | 2023-11-30 |
| Detector | DECTRIS PILATUS3 2M |
| Wavelength(s) | 0.9654 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 37.173, 56.848, 57.378 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 40.380 - 1.140 |
| R-factor | 0.14112 |
| Rwork | 0.140 |
| R-free | 0.16852 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.695 |
| Data reduction software | autoPROC |
| Data scaling software | autoPROC |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0415) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 40.384 | 1.155 |
| High resolution limit [Å] | 1.136 | 1.136 |
| Rmeas | 0.100 | 1.911 |
| Number of reflections | 45461 | 2246 |
| <I/σ(I)> | 7.2 | 1 |
| Completeness [%] | 99.7 | 99.2 |
| Redundancy | 5.5 | |
| CC(1/2) | 0.991 | 0.336 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 4.5 | 293 | 0.15M Lithium chloride, 0.1M Sodium acetate pH 4.5, 32% v/v PEG 400, 0.1M Cadmium chloride |
