6XYK
Crystal structure of bovine trypsin at room temperature.
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | MAX IV BEAMLINE BioMAX |
Synchrotron site | MAX IV |
Beamline | BioMAX |
Temperature [K] | 295 |
Detector technology | PIXEL |
Collection date | 2019-05-09 |
Detector | DECTRIS EIGER X 16M |
Wavelength(s) | 0.6 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 54.830, 58.580, 67.410 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 29.290 - 1.500 |
R-factor | 0.14512746475 |
Rwork | 0.144 |
R-free | 0.16344 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4ih8 |
RMSD bond length | 0.005 |
RMSD bond angle | 0.800 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | PHENIX |
Refinement software | REFMAC (1.11.1_2575) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 29.290 | 1.540 |
High resolution limit [Å] | 1.500 | 1.500 |
Number of reflections | 35707 | 2587 |
<I/σ(I)> | 20.41 | |
Completeness [%] | 100.0 | |
Redundancy | 13.4 | |
CC(1/2) | 0.998 | 0.986 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 293 | 18% PEG8000, 50 mM HEPES pH 7.0, 0.2 M Ammonium sulfate, 3 mM CaCl2and 6 mg/ml benzamidine |