3ER5
THE ACTIVE SITE OF ASPARTIC PROTEINASES
Experimental procedure
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 43.100, 75.400, 42.800 |
| Unit cell angles | 90.00, 97.00, 90.00 |
Refinement procedure
| Resolution | 10.000 - 1.800 |
| R-factor | 0.152 * |
| Rwork | 0.150 |
| RMSD bond length | 0.020 |
| RMSD bond angle | 0.040 |
| Refinement software | PROLSQ |
Data quality characteristics
| Overall | |
| High resolution limit [Å] | 1.800 * |
| Total number of observations | 36927 * |
| Number of reflections | 23224 * |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Batch method * | 4.5 * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | 1 | protein | 60 (mM) | |
| 2 | 1 | 1 | acetate | 0.1 (M) | |
| 3 | 1 | 1 | pepstatin | 600 (mM) | |
| 4 | 1 | 1 | ammonium sulfate | 2.2 (M) |
