1GUB
Hinge-bending motion of D-allose binding protein from Escherichia coli: three open conformations
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | EMBL/DESY, HAMBURG BEAMLINE BW7B |
| Synchrotron site | EMBL/DESY, HAMBURG |
| Beamline | BW7B |
| Temperature [K] | 100 |
| Spacegroup name | P 4 3 2 |
| Unit cell lengths | 133.100, 133.100, 133.100 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 29.000 * - 3.100 |
| R-factor | 0.284 |
| Rwork | 0.280 |
| R-free | 0.27400 * |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1rpj |
| RMSD bond length | 0.024 * |
| RMSD bond angle | 2.500 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | REFMAC (5.1.19) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 29.000 | 3.160 |
| High resolution limit [Å] | 3.080 | 3.080 |
| Rmerge | 0.094 * | 0.338 * |
| Number of reflections | 625 | |
| <I/σ(I)> | 7.1 | 2.3 |
| Completeness [%] | 99.5 | 99.9 |
| Redundancy | 11.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 7.8 * | pH 9.00 |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 5 (mg/ml) | |
| 2 | 1 | drop | HEPES | 10 (mM) | pH7.8 |
| 3 | 1 | reservoir | PEG2000MME | 20-30 (%) | |
| 4 | 1 | reservoir | Tris-HCl | 0.1 (M) | pH9.0 |
| 5 | 1 | reservoir | 0.01 (M) |
