1O7O
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 |
| Collection date | 2002-04-15 |
| Detector | ADSC CCD |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 45.202, 94.288, 94.675 |
| Unit cell angles | 90.00, 99.10, 90.00 |
Refinement procedure
| Resolution | 50.000 - 1.970 |
| R-factor | 0.181 |
| Rwork | 0.181 |
| R-free | 0.20100 * |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1k4v |
| RMSD bond length | 0.006 |
| RMSD bond angle | 22.900 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | CNS (1.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.090 |
| High resolution limit [Å] | 1.970 | 1.970 |
| Rmerge | 0.056 * | 0.105 * |
| Total number of observations | 281132 * | |
| Number of reflections | 55393 | |
| <I/σ(I)> | 18.08 | 10.8 |
| Completeness [%] | 99.4 | 98.7 * |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 6 * | 16 * | PEG6000, TRIS/HCL, pH 8.00 |
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 |
