3POC
The crystal structure of the D307A mutant of alpha-Glucosidase (FAMILY 31) from Ruminococcus obeum ATCC 29174 in complex with acarbose
Replaces: 3NQQExperimental 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 | 2010-04-22 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.97921 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 67.954, 125.691, 87.968 |
| Unit cell angles | 90.00, 107.62, 90.00 |
Refinement procedure
| Resolution | 41.365 - 1.990 |
| R-factor | 0.1705 |
| Rwork | 0.168 |
| R-free | 0.22460 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3n04 |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.028 |
| 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] | 42.000 | 2.030 |
| High resolution limit [Å] | 1.990 | 2.000 |
| Rmerge | 0.103 | 0.585 |
| Number of reflections | 91803 | |
| <I/σ(I)> | 12.2 | 1.16 |
| Completeness [%] | 96.0 | 84.9 |
| Redundancy | 3.4 | 2.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 5.5 | 289 | 0.1M BIS-TRIS, 25% PEG3350, 10% ACARBOSE, pH 5.5, VAPOR DIFFUSION, SITTING DROP, temperature 289K |
