1R46
Structure of human alpha-galactosidase
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 22-ID |
| Synchrotron site | APS |
| Beamline | 22-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2003-02-23 |
| Detector | MARRESEARCH |
| Wavelength(s) | 1.033 |
| Spacegroup name | P 32 2 1 |
| Unit cell lengths | 88.458, 88.458, 215.482 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 50.000 * - 3.250 |
| R-factor | 0.262 |
| Rwork | 0.262 |
| R-free | 0.30100 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | Homology model derived from 1KTB |
| RMSD bond length | 0.009 |
| RMSD bond angle | 22.800 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | CNS (1.0) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 * | 3.370 |
| High resolution limit [Å] | 3.250 | 3.250 |
| Rmerge | 0.246 | 0.740 |
| Total number of observations | 156309 * | |
| Number of reflections | 16080 * | 1542 * |
| <I/σ(I)> | 9.7 | 2.4 |
| Completeness [%] | 99.8 * | 98.7 |
| Redundancy | 9.7 | 6.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 7.5 * | 293 | 30% PEG 4000, 0.1M TRIS HCL (PH 8.0), 0.2M AMMONIUM SULFATE, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 40 (mg/ml) | |
| 2 | 1 | drop | Tris-HCl | 20 (mM) | pH7.5 |
| 3 | 1 | reservoir | PEG4000 | 30 (%(w/v)) | |
| 4 | 1 | reservoir | Tris-HCl | 100 (mM) | pH8.0 |
| 5 | 1 | reservoir | ammonium sulfate | 200 (mM) |
