1RPJ
CRYSTAL STRUCTURE OF D-ALLOSE BINDING PROTEIN FROM ESCHERICHIA COLI
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Detector | RIGAKU RAXIS IIC |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 33.380, 67.820, 53.590 |
| Unit cell angles | 90.00, 96.71, 90.00 |
Refinement procedure
| Resolution | 29.000 - 1.800 |
| R-factor | 0.194 * |
| Rwork | 0.194 |
| R-free | 0.24500 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2dri |
| RMSD bond length | 0.010 |
| RMSD bond angle | 0.026 |
| Data reduction software | DENZO |
| Data scaling software | CCP4 ((SCALA)) |
| Phasing software | AMoRE |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 29.787 | 1.850 |
| High resolution limit [Å] | 1.800 | 1.800 |
| Rmerge | 0.045 | 0.150 |
| Number of reflections | 21163 | |
| <I/σ(I)> | 10.4 | 5 |
| Completeness [%] | 96.5 | 93.6 |
| Redundancy | 2.8 | 2.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 6.5 | pH 6.5 |
Crystallization Reagents
| ID | crystal ID | solution ID | reagent name | concentration | details |
| 1 | 1 | 1 | PEG 550 | ||
| 2 | 1 | 1 | ZnSO4 | ||
| 3 | 1 | 1 | MES BUFFER |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 10 (mg/ml) | |
| 2 | 1 | drop | HEPES | 10 (mM) | |
| 3 | 1 | reservoir | mPEG550 | 40-60 (%(v/v)) | |
| 4 | 1 | reservoir | zinc sulfate | 0.01 (M) | |
| 5 | 1 | reservoir | MES | 0.1 (M) |
