1UTK
Trypsin specificity as elucidated by LIE calculations, X-ray structures and association constant measurements
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE BM1A |
Synchrotron site | ESRF |
Beamline | BM1A |
Temperature [K] | 120 |
Detector technology | IMAGE PLATE |
Detector | MARRESEARCH |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 71.430, 83.260, 30.870 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 8.000 - 1.530 |
R-factor | 0.1774 |
R-free | 0.22910 |
Structure solution method | OTHER |
RMSD bond length | 0.009 |
RMSD bond angle | 0.024 |
Data reduction software | DENZO |
Data scaling software | SCALA |
Refinement software | SHELXL-97 |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 8.000 |
High resolution limit [Å] | 1.530 |
Rmerge | 0.075 |
Number of reflections | 28246 |
<I/σ(I)> | 2.6 |
Completeness [%] | 99.5 |
Redundancy | 5.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 6 | pH 6.00 |