1BYA
CRYSTAL STRUCTURES OF SOYBEAN BETA-AMYLASE REACTED WITH BETA-MALTOSE AND MALTAL: ACTIVE SITE COMPONENTS AND THEIR APPARENT ROLE IN CATALYSIS
Experimental procedure
| Spacegroup name | P 31 2 1 |
| Unit cell lengths | 86.200, 86.200, 144.200 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 9.000 - 2.200 |
| R-factor | 0.169 |
| Rwork | 0.169 |
| RMSD bond length | 0.020 |
| RMSD bond angle | 2.403 |
| Phasing software | X-PLOR |
| Refinement software | TNT |
Data quality characteristics
| Overall | |
| Total number of observations | 219183 * |
| Number of reflections | 45035 * |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | unknown * | Morita, Y., (1975) J. Biochem., 77, 343. * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | 1 | protein | 140 (mg/ml) | |
| 2 | 1 | 1 | ammonium sulfate | 50 (%sat) |
