1UTL
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 | 44.944, 48.269, 83.102 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 8.000 - 1.700 |
R-factor | 0.176 |
Rwork | 0.176 |
R-free | 0.21600 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1bit |
RMSD bond length | 0.008 |
RMSD bond angle | 1.753 |
Data reduction software | DENZO |
Data scaling software | SCALA |
Phasing software | AMoRE |
Refinement software | X-PLOR |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 8.000 | |
High resolution limit [Å] | 1.700 | |
Rmerge | 0.070 | 0.243 |
Number of reflections | 19106 | |
<I/σ(I)> | 8.3 | 3 |
Completeness [%] | 93.8 | 96.4 |
Redundancy | 2.69 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 6 | pH 6.00 |