1ENT
X-RAY ANALYSES OF ASPARTIC PROTEINASES. THE THREE-DIMENSIONAL STRUCTURE AT 2.1 ANGSTROMS RESOLUTION OF ENDOTHIAPEPSIN
Experimental procedure
Spacegroup name | P 1 21 1 |
Unit cell lengths | 43.000, 75.700, 42.900 |
Unit cell angles | 90.00, 97.10, 90.00 |
Refinement procedure
Resolution | 20.000 * - 2.100* |
R-factor | 0.178 * |
RMSD bond length | 0.009 |
RMSD bond angle | 0.007 |
Refinement software | RESTRAIN |
Data quality characteristics
Overall | |
High resolution limit [Å] | 2.100 * |
Rmerge | 0.074 * |
Total number of observations | 44358 * |
Number of reflections | 19356 * |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | unknown * | 4.6 * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | 1 | protein | 2 (mg/ml) | |
2 | 1 | 1 | sodium acetate | 0.1 (M) | |
3 | 1 | 1 | ammonium sulfate | 55 (%sat) |