1UTJ
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] | 295 |
Detector technology | IMAGE PLATE |
Detector | MARRESEARCH |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 45.030, 48.180, 83.010 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 8.000 - 1.830 |
R-factor | 0.162 |
Rwork | 0.162 |
R-free | 0.20700 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1bit |
RMSD bond length | 0.008 |
RMSD bond angle | 1.497 |
Data reduction software | DENZO |
Data scaling software | SCALA |
Phasing software | AMoRE |
Refinement software | X-PLOR |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 8.000 |
High resolution limit [Å] | 1.830 |
Rmerge | 0.068 |
Number of reflections | 14865 |
<I/σ(I)> | 8.5 |
Completeness [%] | 90.6 |
Redundancy | 4.63 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 6 | pH 6.00 |