2XFR
Crystal structure of barley beta-amylase at atomic resolution
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | DIAMOND BEAMLINE I02 |
| Synchrotron site | Diamond |
| Beamline | I02 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2008-03-08 |
| Detector | ADSC CCD |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 68.830, 71.338, 92.659 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 38.855 - 0.970 |
| R-factor | 0.114 |
| Rwork | 0.113 |
| R-free | 0.13040 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1b1y |
| RMSD bond length | 0.014 |
| RMSD bond angle | 1.565 |
| 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] | 49.530 | 1.020 |
| High resolution limit [Å] | 0.950 | 0.970 |
| Rmerge | 0.100 | 0.390 |
| Number of reflections | 253864 | |
| <I/σ(I)> | 2.32 | 1.72 |
| Completeness [%] | 94.6 | 65.6 |
| Redundancy | 5.28 | 2.09 |
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 |
