1IUD
MALTODEXTRIN-BINDING PROTEIN INSERTION/DELETION MUTANT WITH AN INSERTED B-CELL EPITOPE FROM THE PRES2 REGION OF HEPATITIS B VIRUS
Experimental procedure
| Source type | SYNCHROTRON |
| Source details | LURE BEAMLINE DW32 |
| Synchrotron site | LURE |
| Beamline | DW32 |
| Temperature [K] | 288 |
| Detector technology | IMAGE PLATE |
| Detector | MARRESEARCH |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 61.100, 97.400, 137.600 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 6.000 - 2.700 |
| R-factor | 0.178 |
| Rwork | 0.178 |
| R-free | 0.28100 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | WILD-TYPE MALTOSE-BINDING PROTEIN |
| RMSD bond length | 0.012 |
| RMSD bond angle | 24.000 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | X-PLOR (3.1) |
| Refinement software | X-PLOR (3.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 10.000 | 2.800 |
| High resolution limit [Å] | 2.700 | 2.700 |
| Rmerge | 0.054 | 0.367 |
| Number of reflections | 11201 | 1108 * |
| <I/σ(I)> | 14.3 | 3.1 |
| Completeness [%] | 99.0 | 97 |
| Redundancy | 3.6 | 3.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 8.5 * | 17 * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | PEG6000 | 15 (%) | can be replaced by PEG8000 |
| 2 | 1 | drop | Tris-HCl | 10 (mM) | |
| 3 | 1 | drop | 100 (mM) | ||
| 4 | 1 | drop | 3 (mM) | ||
| 5 | 1 | drop | maltose | 1 (mM) | |
| 6 | 1 | drop | protein | 3 (mg/ml) | |
| 7 | 1 | reservoir | PEG | 22 (%) |
