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 |