1GHB
A SECOND ACTIVE SITE IN CHYMOTRYPSIN? THE X-RAY CRYSTAL STRUCTURE OF N-ACETYL-D-TRYPTOPHAN BOUND TO GAMMA-CHYMOTRYPSIN
Experimental procedure
Spacegroup name | P 42 21 2 |
Unit cell lengths | 69.600, 69.600, 97.510 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 5.000 * - 2.200* |
R-factor | 0.152 |
Rwork | 0.152 |
RMSD bond length | 0.010 |
RMSD bond angle | 1.606 |
Phasing software | X-PLOR |
Refinement software | X-PLOR |
Data quality characteristics
Overall | |
High resolution limit [Å] | 2.200 * |
Rmerge | 0.140 * |
Number of reflections | 15361 * |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Batch method * | 5.6 * | Yennawar, N. H., (1994) Biochemistry, 33, 7326. * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | 1 | chymotrypsin | 15 (mg/ml) | |
2 | 1 | 1 | sodium cacodylate | 10 (mM) | |
3 | 1 | 1 | cetyltrimethylammonium bromide | 0.75 (%sat) | |
4 | 1 | 1 | ammonium sulfate | 45 (%sat) | |
5 | 1 | 2 | ammonium sulphate | 65 (%sat) |