Dehydration converts DsbG crystal diffraction from low to high resolution
| Contribuinte(s) |
Hendrickson Wayne A |
|---|---|
| Data(s) |
01/01/2003
|
| Resumo |
Diffraction quality crystals are essential for crystallographic studies of protein structure, and the production of poorly diffracting crystals is often regarded as a dead end in the process. Here we show a dramatic improvement of poorly diffracting DsbG crystals allowing high-resolution diffraction data measurement. Before dehydration, the crystals are fragile and the diffraction pattern is streaky, extending to 10 Angstrom resolution. After dehydration, there is a spectacular improvement, with the diffraction pattern extending to 2 Angstrom resolution. This and other recent results show that dehydration is a simple, rapid, and inexpensive approach to convert poor quality crystals into diffraction quality crystals. |
| Identificador | |
| Idioma(s) |
eng |
| Publicador |
Cell Press |
| Palavras-Chave | #Biochemistry & Molecular Biology #Biophysics #Cell Biology #Crystal Dehydration #X-ray Diffraction #Dsb Proteins #Disulfide Isomerase #Disulfide Bond Formation #Escherichia-coli #Tetragonal Lysozyme #Chaperone Activity #Formation Invivo #In-vivo #Quality #Crystallization #Isomerase #Pathway #C1 #279999 Biological Sciences not elsewhere classified #780105 Biological sciences #060112 Structural Biology (incl. Macromolecular Modelling) |
| Tipo |
Journal Article |