Affinity tags can reduce merohedral twinning of membrane protein crystals
Author
Summary, in English
This work presents a comparison of the crystal packing of three eukaryotic membrane proteins: human aquaporin 1, human aquaporin 5 and a spinach plasma membrane aquaporin. All were purified from expression constructs both with and without affinity tags. With the exception of tagged aquaporin 1, all constructs yielded crystals. Two significant effects of the affinity tags were observed: crystals containing a tag typically diffracted to lower resolution than those from constructs encoding the protein sequence alone and constructs without a tag frequently produced crystals that suffered from merohedral twinning. Twinning is a challenging crystallographic problem that can seriously hinder solution of the structure. Thus, for integral membrane proteins, the addition of an affinity tag may help to disrupt the approximate symmetry of the protein and thereby reduce or avoid merohedral twinning.
Department/s
Publishing year
2008
Language
English
Pages
1183-1186
Publication/Series
Acta Crystallographica. Section D: Biological Crystallography
Volume
64
Document type
Journal article
Publisher
John Wiley & Sons Inc.
Topic
- Structural Biology
Status
Published
ISBN/ISSN/Other
- ISSN: 1399-0047