9IW4
Crystal Structure Sensory Appendage Proteins 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 | C 1 2 1 |
| Unit cell lengths | 77.377, 37.374, 41.014 |
| Unit cell angles | 90.00, 117.04, 90.00 |
Refinement procedure
| Resolution | 36.530 - 1.341 |
| R-factor | 0.1896 |
| Rwork | 0.189 |
| R-free | 0.20010 |
| Structure solution method | SAD |
| RMSD bond length | 0.005 |
| RMSD bond angle | 0.717 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | AutoSol |
| Refinement software | PHENIX ((1.15rc1_3423: ???)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 36.530 | 1.390 |
| High resolution limit [Å] | 1.340 | 1.340 |
| Rmerge | 0.060 | 1.733 |
| Rmeas | 0.067 | 2.089 |
| Rpim | 0.029 | 1.136 |
| Total number of observations | 106372 | 4068 |
| Number of reflections | 22330 | 1429 |
| <I/σ(I)> | 11.2 | 0.5 |
| Completeness [%] | 94.9 | |
| Redundancy | 4.8 | 2.8 |
| CC(1/2) | 0.999 | 0.251 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 293 | 0.1M Lithium chloride, 0.1M Sodium acetate pH 4.5, 30% v/v PEG 400, 0.1M Cadmium chloride |
