2APR
STRUCTURE AND REFINEMENT AT 1.8 ANGSTROMS RESOLUTION OF THE ASPARTIC PROTEINASE FROM RHIZOPUS CHINENSIS
Replaces: 1APRExperimental procedure
Spacegroup name | P 21 21 21 |
Unit cell lengths | 60.310, 60.600, 106.970 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | ? - 1.800 |
R-factor | 0.143 |
RMSD bond length | 0.010 |
RMSD bond angle | 0.034 * |
Refinement software | PROLSQ |
Data quality characteristics
Overall | |
High resolution limit [Å] | 1.800 * |
Rmerge | 0.043 * |
Total number of observations | 129693 * |
Number of reflections | 38090 * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | 1 | calcium acetate solution | 20 (mM) | |
2 | 1 | 1 | protein | 50 (mg/ml) |