1X38
crystal structure of barley beta-D-glucan glucohydrolase isoenzyme exo1 in complex with gluco-phenylimidazole
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 14-ID-B |
| Synchrotron site | APS |
| Beamline | 14-ID-B |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2004-03-29 |
| Detector | MARRESEARCH |
| Wavelength(s) | 1.127 |
| Spacegroup name | P 43 21 2 |
| Unit cell lengths | 100.558, 100.558, 182.414 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 34.300 - 1.698 |
| R-factor | 0.1599 |
| Rwork | 0.160 |
| R-free | 0.18301 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1lq2 |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.326 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | CCP4 |
| Refinement software | REFMAC (5.2.0011) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 34.300 | 1.760 |
| High resolution limit [Å] | 1.700 | 1.700 |
| Rmerge | 0.054 | 0.631 |
| Number of reflections | 98154 | |
| <I/σ(I)> | 42.3 | 3.4 |
| Completeness [%] | 99.8 | 98.6 |
| Redundancy | 12.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7 | 277 | AMMONIUM SULPHATE, PEG 400, SODIUM ACETATE, HEPES-NAOH, pH 7.00, VAPOR DIFFUSION, HANGING DROP, temperature 277K |
