2LPR
STRUCTURAL BASIS FOR BROAD SPECIFICITY IN ALPHA-LYTIC PROTEASE MUTANTS
Experimental procedure
| Spacegroup name | P 32 2 1 |
| Unit cell lengths | 66.250, 66.250, 80.180 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | ? - 2.250 |
| R-factor | 0.127 |
| RMSD bond length | 0.016 |
| RMSD bond angle | 0.053 |
| Refinement software | PROLSQ |
Data quality characteristics
| Overall | |
| High resolution limit [Å] | 2.250 |
| Completeness [%] | 87.0 * |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion * | 8 * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | ||
| 2 | 1 | reservior | lithium sulfate | 1.3 (M) | |
| 3 | 1 | reservoir | Tris-sulfate | 20 (mM) |
