1HT6
CRYSTAL STRUCTURE AT 1.5A RESOLUTION OF THE BARLEY ALPHA-AMYLASE ISOZYME 1
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE BM30A |
| Synchrotron site | ESRF |
| Beamline | BM30A |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2000-05-17 |
| Detector | MARRESEARCH |
| Wavelength(s) | 0.9761 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 88.360, 72.820, 61.740 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 41.600 * - 1.500 |
| Rwork | 0.136 |
| R-free | 0.16300 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | AMY1 structure solved at 2.0A resolution (unpublished results) |
| RMSD bond length | 0.017 |
| RMSD bond angle | 1.700 |
| Data reduction software | DENZO |
| Data scaling software | SCALA |
| Phasing software | AMoRE |
| Refinement software | CNS (1.0) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 41.600 | 1.540 |
| High resolution limit [Å] | 1.500 | 1.500 |
| Rmerge | 0.045 | 0.119 |
| Total number of observations | 271695 * | |
| Number of reflections | 63366 | |
| <I/σ(I)> | 13.3 | 6.2 |
| Completeness [%] | 98.7 | 97.3 |
| Redundancy | 4.3 | 3.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.7 | 290 * | Robert, X., (2002) Acta Crystallogr., D58, 683. * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 5.1 (mg/ml) | |
| 2 | 1 | drop | 2-propanol | 3 (%(v/v)) | |
| 3 | 1 | reservoir | PEG8000 | 20 (%(w/v)) |
