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Diffraction grade crystals of Escherichia coli serine hydroxymethyltransferase
P Stover1, H Kruschwitz, V Schirch
1Department of Biochemistry and Molecular Biophysics, Virginia Commonwealth University, Richmond 23298-0614.
Journal of Molecular Biology
|April 5, 1993
Abstract:
Diffraction grade crystals of serine hydroxymethyltransferase were obtained after extensive screening of source of enzyme, purification procedures, ligand binding and crystallization conditions. Serine hydroxymethyltransferase purified from Escherichia coli crystallizes in two forms that are suitable for crystal structure determination.