3GCT
STRUCTURE OF GAMMA-*CHYMOTRYPSIN IN THE RANGE $P*H 2.0 TO $P*H 10.5 SUGGESTS THAT GAMMA-CHYMOTRYPSIN IS A COVALENT ACYL-ENZYME ADDUCT AT LOW $P*H
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Temperature [K] | 285 |
Detector technology | FILM |
Detector | KODAK |
Spacegroup name | P 42 21 2 |
Unit cell lengths | 70.000, 70.000, 97.700 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 10.000 - 1.600 |
Rwork | 0.173 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.019 * |
RMSD bond angle | 17.500 * |
Data reduction software | OSCTST |
Data scaling software | AGROVATA/ROTAVATE |
Refinement software | TNT |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 10.000 * |
High resolution limit [Å] | 1.600 * |
Rmerge | 0.066 * |
Total number of observations | 58476 * |
Number of reflections | 23255 * |
Completeness [%] | 70.3 * |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Batch method * | 7 * | pH 10.5 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | 1 | ammonium sulfate | 50 (%sat) |