| Literature DB >> 8135821 |
T A Keller1, T Ferenci, A Prilipov, J P Rosenbusch.
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.Entities:
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Year: 1994 PMID： 8135821 DOI： 10.1006/bbrc.1994.1295
Source DB: PubMed Journal: Biochem Biophys Res Commun ISSN： 0006-291X Impact factor: 3.575