2ECP
THE CRYSTAL STRUCTURE OF THE E. COLI MALTODEXTRIN PHOSPHORYLASE COMPLEX
Experimental procedure
| Source type | SYNCHROTRON |
| Source details | ELETTRA BEAMLINE 5.2R |
| Synchrotron site | ELETTRA |
| Beamline | 5.2R |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Detector | MAR scanner 180 mm plate |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 76.490, 105.840, 217.720 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 15.000 - 2.950 |
| R-factor | 0.241 * |
| Rwork | 0.241 |
| R-free | 0.29300 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.009 * |
| RMSD bond angle | 2.100 * |
| Data reduction software | MOSFLM |
| Data scaling software | CCP4 ((SCALA)) |
| Phasing software | AMoRE |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 33.600 | 3.110 |
| High resolution limit [Å] | 2.950 | 2.950 |
| Rmerge | 0.068 | 0.157 |
| Number of reflections | 33657 | |
| <I/σ(I)> | 12.5 | 5.3 |
| Completeness [%] | 88.9 | 78.2 |
| Redundancy | 2.6 | 2.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 8.5 | 18 * | pH 8.5 |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 10 (mg/ml) | |
| 2 | 1 | reservoir | acarbose | 30 (mM) | |
| 3 | 1 | reservoir | PEG3350 | 25-28 (%(w/v)) | |
| 4 | 1 | reservoir | 0.1-0.6 (M) | ||
| 5 | 1 | reservoir | Tris-HCl | 0.1 (M) |
