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Affinity tags can reduce merohedral twinning of membrane protein crystals

Anna Backmark (Institutionen för kemi- och bioteknik) ; Maria Nyblom (Institutionen för kemi- och bioteknik, Molekylär mikroskopi) ; Susanna Törnroth-Horsefield ; Urszula Kosinska-Eriksson ; Kristina Hedfalk ; Karin Lindkvist-Petersson ; Richard Neutze ; Rob Horsefield
Acta Crystallogarphis D Vol. D64 (2008), p. 1183-1186.
[Artikel, refereegranskad vetenskaplig]

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.



Denna post skapades 2008-11-19. Senast ändrad 2011-01-20.
CPL Pubid: 78414

 

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Institutioner (Chalmers)

Institutionen för kemi- och bioteknik (2005-2014)
Institutionen för kemi- och bioteknik, Molekylär mikroskopi (2008-2014)
Institutionen för kemi (2001-2011)
Institutionen för cell- och molekylärbiologi (1994-2011)

Ämnesområden

Kemi
Biologiska vetenskaper

Chalmers infrastruktur