1LU1
THE STRUCTURE OF THE DOLICHOS BIFLORUS SEED LECTIN IN COMPLEX WITH THE FORSSMAN DISACCHARIDE
Experimental procedure
Source type | ROTATING ANODE |
Source details | RIGAKU |
Temperature [K] | 293 |
Detector technology | IMAGE PLATE |
Collection date | 1998-02 |
Detector | MARRESEARCH |
Spacegroup name | I 41 2 2 |
Unit cell lengths | 79.050, 79.050, 260.110 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.000 - 2.600 |
R-factor | 0.194 |
Rwork | 0.194 |
R-free | 0.23400 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1fat |
RMSD bond length | 0.080 * |
RMSD bond angle | 1.460 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | X-PLOR (3.851) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 2.620 |
High resolution limit [Å] | 2.600 | 2.600 |
Rmerge | 0.146 * | 0.750 |
Total number of observations | 91892 * | |
Number of reflections | 13175 | |
<I/σ(I)> | 15.2 | 2.27 |
Completeness [%] | 99.9 | 99.9 |
Redundancy | 7 | 7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 7.5 | 100 MM HEPES PH 7.5 0.2 M MGCL2 30% (W/V) PEG 400 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 5 (mg/ml) | |
2 | 1 | drop | adenine | 5 (mM) | |
3 | 1 | reservoir | HEPES | 100 (mM) | |
4 | 1 | reservoir | 0.2 (M) | ||
5 | 1 | reservoir | PEG400 | 30 (%(w/v)) |