3K02
Crystal structures of the GacH receptor of Streptomyces glaucescens GLA.O in the unliganded form and in complex with acarbose and an acarbose homolog. Comparison with acarbose-loaded maltose binding protein of Salmonella typhimurium.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | BESSY BEAMLINE 14.1 |
| Synchrotron site | BESSY |
| Beamline | 14.1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2008-10-21 |
| Detector | ADSC QUANTUM 210 |
| Wavelength(s) | 0.91841 |
| Spacegroup name | P 41 21 2 |
| Unit cell lengths | 72.177, 72.177, 160.454 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 50.000 - 1.550 |
| R-factor | 0.207 |
| Rwork | 0.205 |
| R-free | 0.24300 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.417 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 65.800 | 50.000 | 1.610 |
| High resolution limit [Å] | 1.550 | 3.340 | 1.550 |
| Rmerge | 0.046 | 0.029 | 0.452 |
| Number of reflections | 60053 | ||
| <I/σ(I)> | 18.2 | ||
| Completeness [%] | 97.0 | 96.6 | 83.7 |
| Redundancy | 4.1 | 4.2 | 3.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 4 | 291 | 2.5 M (NH4)2SO4, 100 mM citric acid, pH 4.0, VAPOR DIFFUSION, HANGING DROP, temperature 291K |
