1C5I
HYDROGEN BONDING AND CATALYSIS: AN UNEXPECTED EXPLANATION FOR HOW A SINGLE AMINO ACID SUBSTITUTION CAN CHANGE THE PH OPTIMUM OF A GLYCOSIDASE
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU300 |
Temperature [K] | 298 |
Detector technology | IMAGE PLATE |
Detector | RIGAKU RAXIS IIC |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 43.830, 52.740, 78.800 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 10.000 - 1.800 |
R-factor | 0.193 |
Rwork | 0.193 |
Structure solution method | OTHER |
RMSD bond length | 0.007 |
RMSD bond angle | 1.136 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | X-PLOR |
Refinement software | X-PLOR (3.851) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 9999.000 * | |
High resolution limit [Å] | 1.800 | 1.800 * |
Rmerge | 0.073 | 0.142 * |
Total number of observations | 99311 * | |
Number of reflections | 17579 | |
<I/σ(I)> | 25.8 | |
Completeness [%] | 99.9 | |
Redundancy | 5.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 7.5 | Sidhu, G., (1999) J. Mol. Biol., 38, 5346. * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 15 (mg/ml) | |
2 | 1 | reservoir | ammonium sulfate | 17 (%) | |
3 | 1 | reservoir | 10 (mM) | ||
4 | 1 | reservoir | Tris-HCl | 40 (mM) |