6AVL
Orthorhombic Trypsin (295 K) in the presence of 50% xylose
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SEALED TUBE |
Source details | OXFORD DIFFRACTION NOVA |
Temperature [K] | 295 |
Detector technology | CCD |
Collection date | 2017-06-01 |
Detector | OXFORD ONYX CCD |
Wavelength(s) | 1.54 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 54.870, 58.756, 67.484 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 13.468 - 2.000 |
R-factor | 0.1526 |
Rwork | 0.150 |
R-free | 0.20490 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.007 |
RMSD bond angle | 0.871 |
Data reduction software | CrysalisPro |
Data scaling software | SCALA |
Refinement software | PHENIX |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 13.790 | 2.110 |
High resolution limit [Å] | 2.000 | 2.000 |
Number of reflections | 15148 | |
<I/σ(I)> | 5.4 | |
Completeness [%] | 99.2 | |
Redundancy | 3.7 | |
CC(1/2) | 0.980 | 0.870 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8 | 295 | 0.1 M Tris buffer 0.2 M AmSO4 25% (w/v) PEG 8000 0.1 M benzamidine-HCl Protein 40 mg/mL in water |