2O9O
Crystal Structure of the buffalo Secretory Signalling Glycoprotein at 2.8 A resolution
Replaces: 1SV8Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU300 |
Temperature [K] | 278 |
Detector technology | IMAGE PLATE |
Collection date | 2003-12-10 |
Detector | MARRESEARCH |
Wavelength(s) | 1.5418 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 63.100, 66.859, 108.543 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.000 - 2.800 |
R-factor | 0.18843 |
Rwork | 0.186 |
R-free | 0.23619 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2esc |
RMSD bond length | 0.019 |
RMSD bond angle | 1.865 |
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] | 20.000 | 2.850 |
High resolution limit [Å] | 2.800 | 2.800 |
Number of reflections | 11349 | |
<I/σ(I)> | 11 | 2.7 |
Completeness [%] | 97.1 | 95.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.8 | 298 | TRIS-HCL, NACL, 19% ETHANOL, pH 7.8, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K |