5C2M
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 | 2009-11-09 |
| Detector | RIGAKU RAXIS IV++ |
| Wavelength(s) | 1.5417 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 44.693, 60.929, 88.351 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 50.000 - 1.900 |
| R-factor | 0.1929 |
| Rwork | 0.191 |
| R-free | 0.23485 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1tl2 |
| RMSD bond length | 0.024 |
| RMSD bond angle | 1.902 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.5.0088) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.930 |
| High resolution limit [Å] | 1.900 | 1.900 |
| Rmerge | 0.303 | |
| Number of reflections | 19656 | |
| <I/σ(I)> | 29.6 | 2.6 |
| Completeness [%] | 99.8 | 97.4 |
| Redundancy | 6.1 | 4.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | MICROBATCH | 292 | 0.1M NaF, 0.05 M Bis-Tris propane pH 7.5, 10% polyethylene glycol 3,350. |
