1IEX
Crystal structure of barley beta-D-glucan glucohydrolase isoenzyme Exo1 in complex with 4I,4III,4V-S-trithiocellohexaose
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | PHOTON FACTORY BEAMLINE BL-6A |
| Synchrotron site | Photon Factory |
| Beamline | BL-6A |
| Temperature [K] | 255 |
| Detector technology | DIFFRACTOMETER |
| Collection date | 1998-03-01 |
| Detector | WEISSENBERG |
| Wavelength(s) | 1.0 |
| Spacegroup name | P 43 21 2 |
| Unit cell lengths | 102.420, 102.420, 185.480 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 12.000 - 2.200 |
| R-factor | 0.1776 * |
| Rwork | 0.178 |
| R-free | 0.21090 * |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1ex1 |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.300 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | CNS |
| Refinement software | CNS |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 20.000 |
| High resolution limit [Å] | 2.200 | 2.200 |
| Rmerge | 0.098 | 0.486 |
| Total number of observations | 123698 * | |
| Number of reflections | 46444 | |
| <I/σ(I)> | 15.8 | |
| Completeness [%] | 83.4 | 55.8 |
| Redundancy | 4.40 * |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7 | 277-279 * | Hrmova, M., (1998) Acta Cryst., D54, 687. * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | enzyme | 6.8 (mg/ml) | |
| 2 | 1 | drop | HEPES-NaOH | 75 (mM) | |
| 3 | 1 | drop | sodium acetate | 7.5 (mM) | |
| 4 | 1 | drop | PEG400 | 1.2 (%(w/v)) | |
| 5 | 1 | drop | ammonium sulfate | 0.8 (M) | |
| 6 | 1 | reservoir | ammonium sulfate | 1.7 (M) | |
| 7 | 1 | reservoir | HEPES-NaOH | 50 (mM) |
