Affordable Access

Publisher Website

Crystallization of Monodisperse Maltoporin from Wild-Type and Mutant Strains of Various Enterobacteriaceae

Authors
Journal
Biochemical and Biophysical Research Communications
0006-291X
Publisher
Elsevier
Publication Date
Volume
199
Issue
2
Identifiers
DOI: 10.1006/bbrc.1994.1295
Disciplines
  • Biology

Abstract

Abstract Maltoporin has been purified by affinity chromatography on starch gel columns. This single-step procedure affords the rapid purification of active protein from wild-type and mutants of E. coli, and from other Gram-negative bacteria. The monodisperse protein was crystallized under various conditions. Several preparations have yielded crystals amendable to X-ray analysis, notably a single cysteine substitution, S57C.

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