Dehydration converts DsbG crystal diffraction from low to high resolution


Autoria(s): Heras, B.; Edeling, M. A.; Byriel, K. A.; Jones, A.; Raina, S.; Martin, J. L.
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

http://espace.library.uq.edu.au/view/UQ:66113

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