3TMN
THE BINDING OF L-VALYL-L-TRYPTOPHAN TO CRYSTALLINE THERMOLYSIN ILLUSTRATES THE MODE OF INTERACTION OF A PRODUCT OF PEPTIDE HYDROLYSIS
Experimental procedure
Experimental method | SINGLE CRYSTAL |
Source type | ROTATING ANODE |
Source details | ELLIOTT GX-21 |
Temperature [K] | 285 |
Detector technology | FILM |
Collection date | 1988 |
Detector | KODAK |
Spacegroup name | P 61 2 2 |
Unit cell lengths | 94.100, 94.100, 131.400 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 10.000 - 1.700 |
R-factor | 0.173 |
Structure solution method | MOLECULAR SUPSTATUTION |
RMSD bond length | 0.016 |
RMSD bond angle | 3.200 |
Data reduction software | OSCTST |
Data scaling software | AGROVATA/ROTAVATE |
Refinement software | TNT |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 29.800 |
High resolution limit [Å] | 1.700 |
Rmerge | 0.049 |
Total number of observations | 45350 * |
Number of reflections | 28779 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | unknown * | 7.2 | pH 7.2 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | 1 | calcium acetate | 10 (mM) | |
2 | 1 | 1 | Tris | 10 (mM) | |
3 | 1 | 1 | dimethylsulfoxide | 7 (%(v/v)) |