2B31
Crystal structure of the complex formed between goat signalling protein with pentasaccharide at 3.1 A resolution reveals large scale conformational changes in the residues of TIM barrel
Replaces: 1ZU9Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU300 |
Temperature [K] | 298 |
Detector technology | IMAGE PLATE |
Collection date | 2005-05-14 |
Detector | MARRESEARCH |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 62.745, 66.613, 107.812 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 56.700 - 3.100 |
R-factor | 0.17859 |
Rwork | 0.177 |
R-free | 0.21782 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1QZO |
RMSD bond length | 0.020 |
RMSD bond angle | 2.440 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | REFMAC (5.0) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 56.700 | 3.210 |
High resolution limit [Å] | 3.100 | 3.100 |
Number of reflections | 8493 | |
<I/σ(I)> | 7 | 2.4 |
Completeness [%] | 98.5 | 99.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 7.8 | 298 | 25mM Tris HCl, 50mM NaCl, 19% ethanol, pH 7.8, VAPOR DIFFUSION, HANGING DROP, temperature 298.0 K, pH 7.80 |