1URD
X-ray structures of the maltose-maltodextrin binding protein of the thermoacidophilic bacterium Alicyclobacillus acidocaldarius provide insight into acid stability of proteins
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-4 |
| Synchrotron site | ESRF |
| Beamline | ID14-4 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2000-12-15 |
| Detector | ADSC CCD |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 49.230, 70.783, 104.671 |
| Unit cell angles | 90.00, 96.58, 90.00 |
Refinement procedure
| Resolution | 40.000 - 1.530 |
| R-factor | 0.206 |
| Rwork | 0.206 |
| R-free | 0.23100 |
| Structure solution method | MAD |
| RMSD bond length | 0.005 |
| RMSD bond angle | 1.190 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | CNS (1.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 40.000 | 1.560 |
| High resolution limit [Å] | 1.530 | 1.530 |
| Rmerge | 0.083 | 0.187 |
| Number of reflections | 99996 | |
| <I/σ(I)> | 11.9 | 5.8 |
| Completeness [%] | 98.8 | 88.3 |
| Redundancy | 5.2 | 2.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, sitting drop * | 7.2 * | 18 * | PEG 5000, TRIS-HCL, AMMONIUM SULPHATE, pH 8.00 |
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 |
