2GCT
STRUCTURE OF GAMMA-CHYMOTRYPSIN IN THE RANGE PH 2.0 TO PH 10.5 SUGGESTS THAT GAMMA-CHYMOTRYPSIN IS A COVALENT ACYL-ENZYME ADDUCT AT LOW PH
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 | 69.800, 69.800, 98.100 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 10.000 - 1.800 |
Rwork | 0.169 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.019 |
RMSD bond angle | 18.100 * |
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] | 1.800 * |
Rmerge | 0.068 * |
Total number of observations | 17029 * |
Number of reflections | 13431 * |
Completeness [%] | 63.2 * |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Batch method * | 7 * | pH 2.0 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | 1 | ammonium sulfate | 50 (%sat) |