1OA3
Comparison of Family 12 Glycoside Hydrolases and Recruited Substitutions Important for Thermal Stability
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-4 |
Synchrotron site | ESRF |
Beamline | ID14-4 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2000-04-29 |
Detector | ADSC CCD |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 62.490, 77.547, 83.410 |
Unit cell angles | 90.00, 98.46, 90.00 |
Refinement procedure
Resolution | 29.000 - 1.700 |
R-factor | 0.1927 |
Rwork | 0.192 |
R-free | 0.21700 * |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1h8v |
RMSD bond length | 0.011 * |
RMSD bond angle | 1.300 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 1.730 |
High resolution limit [Å] | 1.700 | 1.700 |
Rmerge | 0.097 * | 0.126 * |
Total number of observations | 346287 * | |
Number of reflections | 85680 | |
<I/σ(I)> | 14 | 5.7 |
Completeness [%] | 98.9 | 84.6 |
Redundancy | 4.0 * |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 6 | 20-24 * | pH 6.00 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | reservoir | cacodylate | 200 (mM) | pH6.0 |
2 | 1 | reservoir | ammonium acetate | 200 (mM) | |
3 | 1 | reservoir | PEG2000MME | 10-30 (%(w/w)) | |
4 | 1 | drop | protein | 15 (mg/ml) |