3LNW
Close correlation of protein thermostability and self-buried area rate revealed by crystal structure of HPr from Thermoanaerobacter tengcongensis MB4
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU |
Temperature [K] | 277 |
Detector technology | IMAGE PLATE |
Detector | RIGAKU |
Wavelength(s) | 1.5418 |
Spacegroup name | P 31 |
Unit cell lengths | 67.972, 67.972, 50.444 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 38.304 - 2.302 |
R-factor | 0.1919 |
Rwork | 0.190 |
R-free | 0.22060 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.010 |
RMSD bond angle | 1.376 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Refinement software | PHENIX ((phenix.refine: 1.5_2)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.380 |
High resolution limit [Å] | 2.300 | 2.300 |
Rmerge | 0.072 | 0.245 |
Number of reflections | 11556 | |
<I/σ(I)> | 24.271 | 8.404 |
Completeness [%] | 99.9 | 100 |
Redundancy | 5.5 | 5.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 277 | 15% PEG 20000, 0.1M MES, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K |