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) |






