Affinity tags can reduce merohedral twinning of membrane protein crystals

Forskningsoutput: TidskriftsbidragArtikel i vetenskaplig tidskrift

Abstract

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.

Detaljer

Författare
Enheter & grupper
Externa organisationer
  • Chalmers Tekniska Högskola
  • Göteborgs universitet
Forskningsområden

Ämnesklassifikation (UKÄ) – OBLIGATORISK

  • Strukturbiologi
Originalspråkengelska
Sidor (från-till)1183-1186
TidskriftActa Crystallographica. Section D: Biological Crystallography
Volym64
StatusPublished - 2008
PublikationskategoriForskning
Peer review utfördJa