6C9Z
THE CRYSTAL STRUCTURE OF THE alpha-Glucosidase (GH 31) W169Y mutant FROM RUMINOCOCCUS OBEUM ATCC 29174 in complex with voglibose
Experimental 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 | 2013-04-07 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.9792 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 67.751, 126.346, 88.191 |
| Unit cell angles | 90.00, 107.82, 90.00 |
Refinement procedure
| Resolution | 32.250 - 2.101 |
| R-factor | 0.1945 |
| Rwork | 0.192 |
| R-free | 0.24580 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3nuk |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.011 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | HKL-3000 |
| Refinement software | PHENIX (1.8.1_1168) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 33.500 | 2.140 |
| High resolution limit [Å] | 2.100 | 2.100 |
| Rmerge | 0.102 | 0.590 |
| Number of reflections | 79048 | 3701 |
| <I/σ(I)> | 20.7 | 1.9 |
| Completeness [%] | 97.6 | 92.9 |
| Redundancy | 4 | 3.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 5.5 | 277 | 0.1 M Bis-Tris 25% (w/v) PEG3350 |
