Affordable Access

Publisher Website

Crystallization and preliminary X-ray studies ofd-serine dehydratase fromEscherichia coli

Authors
Journal
Journal of Molecular Biology
0022-2836
Publisher
Elsevier
Publication Date
Volume
214
Issue
3
Identifiers
DOI: 10.1016/0022-2836(90)90282-q
Disciplines
  • Biology

Abstract

Abstract Single crystals of d-serine dehydratase from Escherichia coli complexed with 3-amino-2-hydroxypropionate have been obtained from ammonium sulfate solution (pH 7.0) by vapor diffusion. The crystals belong to the trigonal space group P3 1 or P3 2 with a = b = 81.3 A ̊ and c = 58.4 A ̊ . The asymmetric unit cell contains one protein molecule with M r = 48,289. The crystals diffract to at least 3.0 Å resolution and are suitable for X-ray structure analysis.

There are no comments yet on this publication. Be the first to share your thoughts.