1URG
X-ray structures from the maltose-maltodextrin binding protein of the thermoacidophilic bacterium Alicyclobacillus acidocaldarius
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Temperature [K] | 293 |
| Detector technology | IMAGE PLATE |
| Detector | MARRESEARCH |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 50.110, 72.160, 57.780 |
| Unit cell angles | 90.00, 109.63, 90.00 |
Refinement procedure
| Resolution | 50.000 - 1.800 |
| R-factor | 0.194 |
| Rwork | 0.194 |
| R-free | 0.21700 |
| Structure solution method | MAD |
| Starting model (for MR) | 1anf |
| RMSD bond length | 0.005 |
| RMSD bond angle | 1.230 |
| Data reduction software | XDS (V. 2002) |
| Data scaling software | XSCALE (V. 2002) |
| Phasing software | CNS |
| Refinement software | CNS (1.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.900 |
| High resolution limit [Å] | 1.800 | 1.800 |
| Rmerge | 0.155 | 0.524 |
| Number of reflections | 35989 | |
| <I/σ(I)> | 7.5 | 2.1 |
| Completeness [%] | 99.5 | 91.4 |
| Redundancy | 3.9 | 3.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, sitting drop * | 7.2 * | 18 * | pH 9.50 |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 9.6 (mg/ml) | |
| 2 | 1 | drop | Tris-HCl | 50 (mM) | pH7.2 |
| 3 | 1 | drop | glycerol | 5 (%) | |
| 4 | 1 | drop | maltose | 10 (mM) | |
| 5 | 1 | reservoir | PEG8000 | 20 (%(w/v)) | |
| 6 | 1 | reservoir | CHES | 100 (mM) | pH9.5 |
