5TS4
Crystal structure of a de novo designed protein with curved beta-sheet
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 8.2.1 |
| Synchrotron site | ALS |
| Beamline | 8.2.1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2015-10-20 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 1.0 |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 81.307, 101.538, 101.584 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 40.650 - 3.005 |
| R-factor | 0.278 |
| Rwork | 0.274 |
| R-free | 0.31620 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.006 |
| RMSD bond angle | 0.719 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | PHENIX (dev_1616) |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 40.650 |
| High resolution limit [Å] | 3.000 |
| Number of reflections | 8652 |
| <I/σ(I)> | 16 |
| Completeness [%] | 98.0 |
| Redundancy | 8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 298 | 0.1 M Tris hydrochloride, pH 8.5 and 25% PEG 3,350 |
