3T25
TMAO-grown orthorhombic trypsin (bovine)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SEALED TUBE |
Source details | OTHER |
Temperature [K] | 298 |
Detector technology | CCD |
Collection date | 2011-06-28 |
Detector | OXFORD ONYX CCD |
Wavelength(s) | 1.54 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 54.934, 58.576, 67.941 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.570 - 1.700 |
R-factor | 0.15837 |
Rwork | 0.157 |
R-free | 0.18750 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1tpo |
RMSD bond length | 0.014 |
RMSD bond angle | 1.449 |
Data reduction software | CrysalisPro |
Data scaling software | SCALA (3.3.16) |
Refinement software | REFMAC |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 44.400 | 20.568 | 1.790 |
High resolution limit [Å] | 1.700 | 5.380 | 1.700 |
Rmerge | 0.031 | 0.437 | |
Number of reflections | 24788 | ||
<I/σ(I)> | 16.1 | 21.1 | 1.5 |
Completeness [%] | 99.9 | 98.2 | 100 |
Redundancy | 5.3 | 7.4 | 3.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 6 | 298 | 40 mg/mL protein in 50 mM benzamidine, 2 M TMAO, 0.2 M AmSO4, 0.1 M MES, pH 6.0, VAPOR DIFFUSION, SITTING DROP, temperature 298K |