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) |