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. |