5HCF
T. cruzi calreticulin globular domain
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID29 |
| Synchrotron site | ESRF |
| Beamline | ID29 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2014-03-06 |
| Detector | DECTRIS PILATUS3 6M |
| Wavelength(s) | 0.97625 |
| Spacegroup name | P 1 |
| Unit cell lengths | 79.300, 79.380, 85.080 |
| Unit cell angles | 95.57, 98.69, 119.86 |
Refinement procedure
| Resolution | 47.699 - 2.451 |
| R-factor | 0.2246 |
| Rwork | 0.223 |
| R-free | 0.25660 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.004 |
| RMSD bond angle | 0.837 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | PHASER |
| Refinement software | PHENIX (dev_1839) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 82.000 | 2.600 |
| High resolution limit [Å] | 2.450 | 2.450 |
| Number of reflections | 58978 | |
| <I/σ(I)> | 7.14 | 1.58 |
| Completeness [%] | 92.0 | 86.6 |
| Redundancy | 2.1 | 2.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 293 | 40% PEG 4000, 0.2M sodium acetate, 0.1 M Tris-HCl. 1 M Glucose added to the drop (ratio 1 (protein) / 1 (reservoir)/ 1 Glucose) |
