2ONQ
Gbeta1 stabilization by in vitro evolution and computational design
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU |
Temperature [K] | 110 |
Detector technology | IMAGE PLATE |
Collection date | 2005-10-04 |
Detector | MAR scanner 300 mm plate |
Wavelength(s) | 1.5418 |
Spacegroup name | H 3 2 |
Unit cell lengths | 48.412, 48.412, 107.332 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 19.000 - 1.700 |
R-factor | 0.206 |
Rwork | 0.205 |
R-free | 0.22900 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1pga |
RMSD bond length | 0.021 |
RMSD bond angle | 1.819 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | AMoRE |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 39.050 | 1.760 |
High resolution limit [Å] | 1.700 | 1.700 |
Rmerge | 0.030 | 0.220 |
Number of reflections | 5583 | |
<I/σ(I)> | 27.4 | 7.1 |
Completeness [%] | 99.4 | 100 |
Redundancy | 5.6 | 4.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 5 | 293.15 | 50mM sodium acetate, 20mg/ml protein solution mixed in equal volume of crystallization buffer containing 33% PEG monomethylether, 0.1M calcium chloride, pH 5.0, VAPOR DIFFUSION, SITTING DROP, temperature 293.15K |