1O7Q
Roles of Individual Residues of Alpha-1,3 Galactosyltransferases in Substrate Binding and Catalysis
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SRS BEAMLINE PX9.6 |
Synchrotron site | SRS |
Beamline | PX9.6 |
Temperature [K] | 100 |
Detector technology | CCD |
Detector | ADSC CCD |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 45.326, 94.678, 95.006 |
Unit cell angles | 90.00, 99.03, 90.00 |
Refinement procedure
Resolution | 40.000 - 1.300 |
R-factor | 0.1069 |
R-free | 0.15400 * |
Structure solution method | MAD |
Starting model (for MR) | 1gww |
RMSD bond length | 0.013 |
RMSD bond angle | 1.500 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | SHELXL-97 |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 40.000 | 1.350 |
High resolution limit [Å] | 1.300 | 1.300 |
Rmerge | 0.057 * | 0.171 * |
Total number of observations | 1062198 * | |
Number of reflections | 184017 | |
<I/σ(I)> | 15.85 | 4.23 |
Completeness [%] | 94.9 | 67.7 |
Redundancy | 5.77 | 4.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 6 * | 16 * | PEG6000, TRIS/HCL, pH 8.50 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 5 (mg/ml) | |
2 | 1 | drop | MES/NaOH | 20 (mM) | pH6.0 |
3 | 1 | drop | glycerol | 10 (%) | |
4 | 1 | drop | UDP | 10 (mM) | |
5 | 1 | drop | 0.1 (mM) | ||
6 | 1 | reservoir | PEG6000 | 5 (%) | |
7 | 1 | reservoir | Tris-HCl | 0.1 (M) | pH8.0 |