6XRX
Crystal structure of the mosquito protein AZ1 as an MBP fusion
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 22-ID |
| Synchrotron site | APS |
| Beamline | 22-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2016-10-14 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 1.0 |
| Spacegroup name | P 62 |
| Unit cell lengths | 113.013, 113.013, 83.442 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 33.820 - 1.950 |
| R-factor | 0.1778 |
| Rwork | 0.176 |
| R-free | 0.20120 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5t05 4jrb |
| RMSD bond length | 0.003 |
| RMSD bond angle | 0.581 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.16_3549) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.980 |
| High resolution limit [Å] | 1.950 | 1.950 |
| Rmeas | 0.056 | 0.861 |
| Rpim | 0.022 | 0.337 |
| Number of reflections | 44356 | 2211 |
| <I/σ(I)> | 10.9 | 2.26 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 6.6 | 6.5 |
| CC(1/2) | 0.742 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 293 | 20% PEG 1000, 50mM MES, 100mM NaCl, 200mM MgCl2 |
