Diffraction grade crystals of Escherichia coli serine hydroxymethyltransferase. Academic Article

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.

authors

• Stover, Patrick

published proceedings

• J Mol Biol

author list (cited authors)

• Stover, P., Kruschwitz, H., Schirch, V., & Wright, H. T.

citation count

• 4

complete list of authors

• Stover, P||Kruschwitz, H||Schirch, V||Wright, HT

publication date

• April 1993

publisher

• Elsevier  Publisher

published in

• Journal of Molecular Biology  Journal

keywords

• Animals
• Crystallization
• Escherichia Coli
• Glycine Hydroxymethyltransferase
• Rabbits
• X-Ray Diffraction

PubMed Central ID

• 8478924

Digital Object Identifier (DOI)

• 10.1006/jmbi.1993.1225

start page

• 1094

end page

• 1096

volume

• 230

issue

• 3

URL

• http://dx.doi.org/10.1006/jmbi.1993.1225