5C2N
The de novo evolutionary emergence of a symmetrical protein is shaped by folding constraints
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU RU300 |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2014-05-19 |
| Detector | RIGAKU RAXIS IV++ |
| Wavelength(s) | 1.5417 |
| Spacegroup name | P 31 1 2 |
| Unit cell lengths | 112.219, 112.219, 107.290 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 30.180 - 1.650 |
| R-factor | 0.1893 |
| Rwork | 0.186 |
| R-free | 0.24753 |
| RMSD bond length | 0.020 |
| RMSD bond angle | 1.945 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.7.0029) |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 50.000 |
| High resolution limit [Å] | 1.650 |
| Number of reflections | 92166 |
| <I/σ(I)> | 6.7 |
| Completeness [%] | 100.0 |
| Redundancy | 6.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 292 | 0.05 M PCB buffer (2:1:2 ratio of sodium propionate, sodium cacodylate and Bis-Tris propane, pH 7) 12% polyethylene glycol 1,500. |
