1BSI
HUMAN PANCREATIC ALPHA-AMYLASE FROM PICHIA PASTORIS, GLYCOSYLATED PROTEIN
Experimental procedure
Temperature [K] | 298 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 52.910, 68.900, 131.770 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 10.000 - 2.000 |
R-factor | 0.184 |
Rwork | 0.184 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.008 |
RMSD bond angle | 1.450 |
Refinement software | X-PLOR |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | |
High resolution limit [Å] | 2.000 | 2.000 * |
Rmerge | 0.075 | 0.184 * |
Total number of observations | 166575 * | |
Number of reflections | 33646 | |
Completeness [%] | 95.4 | |
Redundancy | 5.0 * | 2.5 * |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 7.5 | pH 7.5 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | reservoir | MPD | 60 (%) | |
2 | 1 | reservoir | cacodylate | 100 (mM) | pH7.5 |
3 | 1 | drop | protein | 2 (mg/ml) |