2XGI
Crystal structure of Barley Beta-Amylase complexed with 3,4- epoxybutyl alpha-D-glucopyranoside
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SRS BEAMLINE PX10.1 |
| Synchrotron site | SRS |
| Beamline | PX10.1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2007-11-12 |
| Detector | MARMOSAIC 225 mm CCD |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 68.631, 71.158, 92.273 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 24.701 - 1.300 |
| R-factor | 0.129 |
| Rwork | 0.128 |
| R-free | 0.15780 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1b1y |
| RMSD bond length | 0.015 |
| RMSD bond angle | 1.586 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | AMoRE |
| Refinement software | REFMAC (5.5.0091) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 26.130 | 1.370 |
| High resolution limit [Å] | 1.160 | 1.300 |
| Rmerge | 0.070 | 0.500 |
| Number of reflections | 109532 | |
| <I/σ(I)> | 6.21 | 1.48 |
| Completeness [%] | 98.0 | 86.8 |
| Redundancy | 6.48 | 3.88 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5.5 | 291 | CRYSTALS WERE GROWN AT 291 K USING THE HANGING DROP VAPOUR DIFFUSION METHOD WITH PROTEIN AT 10 MG PER ML AND A PRECIPITANT COMPRISED OF 14 PERCENT PEG 3350 IN 100 MM BIS-TRIS PROPANE BUFFER AT PH 5.5 |
