6M4C
C. albicans actin interacting protein Aip5
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | AUSTRALIAN SYNCHROTRON BEAMLINE MX1 |
| Synchrotron site | Australian Synchrotron |
| Beamline | MX1 |
| Temperature [K] | 80 |
| Detector technology | PIXEL |
| Collection date | 2019-03-18 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 0.953700 |
| Spacegroup name | P 61 2 2 |
| Unit cell lengths | 95.116, 95.116, 74.119 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 47.600 - 2.650 |
| R-factor | 0.26538 |
| Rwork | 0.259 |
| R-free | 0.30573 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 6abr |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.604 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0258) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.750 |
| High resolution limit [Å] | 2.650 | 2.650 |
| Number of reflections | 5823 | 602 |
| <I/σ(I)> | 30.51 | |
| Completeness [%] | 91.9 | |
| Redundancy | 30.94 | |
| CC(1/2) | 1.000 | 0.840 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.4 | 293 | 0.1M Tris pH 7.4, 0.2M calcium acetate, 12.5% PEG 3000 |
