1C1L
LACTOSE-LIGANDED CONGERIN I
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | PHOTON FACTORY BEAMLINE BL-6A |
Synchrotron site | Photon Factory |
Beamline | BL-6A |
Temperature [K] | 291 |
Detector technology | IMAGE PLATE |
Detector | FUJI |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 95.440, 36.450, 40.160 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 8.000 - 1.500 |
R-factor | 0.213 * |
Rwork | 0.213 |
R-free | 0.26500 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1slt |
RMSD bond length | 0.009 |
RMSD bond angle | 2.400 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | X-PLOR (3.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 1.550 |
High resolution limit [Å] | 1.500 | 1.500 |
Rmerge | 0.068 | |
Number of reflections | 20509 | |
Completeness [%] | 89.0 | 65.5 |
Redundancy | 2.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 7 * | 18 * | pH 9.0 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | reservoir | PEG6000 | 25 (%(w/v)) | |
2 | 1 | reservoir | Tris-HCl | 0.1 (M) | |
3 | 1 | drop | protein | 20 (mg/ml) | |
4 | 1 | drop | lactose solution | 2 (mM) | |
5 | 1 | drop | Tris-HCl | 10 (mM) |