1GAH
GLUCOAMYLASE-471 COMPLEXED WITH ACARBOSE
Experimental procedure
| Source type | ROTATING ANODE |
| Source details | SIEMENS |
| Temperature [K] | 293 |
| Detector technology | AREA DETECTOR |
| Detector | SIEMENS |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 116.800, 104.100, 48.400 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 10.000 - 2.000 |
| R-factor | 0.131 |
| Rwork | 0.131 |
| R-free | 0.15900 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | NATIVE GLUCOAMYLASE |
| RMSD bond length | 0.008 |
| RMSD bond angle | 21.500 * |
| Data reduction software | XENGEN |
| Data scaling software | XENGEN |
| Phasing software | X-PLOR (3.1) |
| Refinement software | X-PLOR (3.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 15.000 | 2.130 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.057 | 0.145 |
| Total number of observations | 87952 * | |
| Number of reflections | 34394 | |
| <I/σ(I)> | 22 | 5.6 |
| Completeness [%] | 85.0 * | 54 * |
| Redundancy | 2.56 | 1.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 6.5 * | Golubev, A. M., (1992) J. Mol. Biol., 226, 271. * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 10-15 (mg/ml) | |
| 2 | 1 | drop | PEG6000 | 30 (%(w/v)) | |
| 3 | 1 | drop | sodium phosphate | 0.15 (M) | |
| 4 | 1 | reservoir | PEG6000 | 30 (%(w/v)) | |
| 5 | 1 | reservoir | sodium phosphate | 0.15 (M) |
