3PHA
The crystal structure of the W169Y mutant of alpha-glucosidase (gh31 family) from Ruminococcus obeum atcc 29174 in complex with acarbose
Replaces: 3NXMExperimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-ID |
| Synchrotron site | APS |
| Beamline | 19-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2010-03-22 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.97929 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 88.032, 125.955, 133.580 |
| Unit cell angles | 90.00, 107.72, 90.00 |
Refinement procedure
| Resolution | 42.415 - 2.173 |
| R-factor | 0.2029 |
| Rwork | 0.200 |
| R-free | 0.26530 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3n04 |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.086 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | MOLREP |
| Refinement software | PHENIX ((phenix.refine: 1.5_2)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 42.500 | 2.220 |
| High resolution limit [Å] | 2.173 | 2.180 |
| Rmerge | 0.109 | 0.580 |
| Number of reflections | 143009 | |
| <I/σ(I)> | 14.4 | 1.4 |
| Completeness [%] | 98.8 | 91.7 |
| Redundancy | 3.6 | 2.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5.5 | 289 | 0.1M BIS-TRIS, 25% PEG3350, 10% ACARBOSE, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 289K |
