5ER2
High-resolution X-ray diffraction study of the complex between endothiapepsin and an oligopeptide inhibitor. the analysis of the inhibitor binding and description of the rigid body shift in the enzyme
Experimental procedure
Spacegroup name | P 1 21 1 |
Unit cell lengths | 42.900, 75.800, 42.900 |
Unit cell angles | 90.00, 96.90, 90.00 |
Refinement procedure
Resolution | 20.000 - 1.800 |
Rwork | 0.160 |
RMSD bond length | 0.012 |
RMSD bond angle | 0.056 |
Refinement software | PROLSQ |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 20.000 * |
High resolution limit [Å] | 1.800 * |
Rmerge | 0.050 * |
Total number of observations | 26706 * |
Number of reflections | 21985 * |
Completeness [%] | 89.0 * |
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 | enzyme | 2 (mg/ml) | |
2 | 1 | 1 | acetate | 0.1 (M) | |
3 | 1 | 2 | ammonium sulfate | 55 (%sat) | |
4 | 1 | 2 | acetone |