Two-dimensional crystallization of a histidine-tagged protein on monolayers of fluidity-enhanced Ni2+-chelating lipids
Protein two-dimensional (2D) crystallization on lipid monolayers is a powerful method for structure determination. This method has been extended using the specific and strong interaction between histidine residues (of an overexpressed protein) and Ni2+ ions tethered at the headgroup of synthetic lip...
Główni autorzy: | Courty, S, Lebeau, L, Martel, L, Lenne, P, Balavoine, F, Dischert, W, Konovalov, O, Mioskowski, C, Legrand, J, Venien-Bryan, C |
---|---|
Format: | Journal article |
Język: | English |
Wydane: |
2002
|
Podobne zapisy
-
Two-dimensional crystallization of a membrane protein on a detergent-resistant lipid monolayer.
od: Lebeau, L, i wsp.
Wydane: (2001) -
Synchrotron radiation diffraction from two-dimensional protein crystals at the air/water interface.
od: Lenne, P, i wsp.
Wydane: (2000) -
A soluble VE-cadherin fragment forms 2D arrays of dimers upon binding to a lipid monolayer.
od: Al-Kurdi, R, i wsp.
Wydane: (2004) -
Synthesis of Ni2+-functionalized polydopamine magnetic beads for facilitated purification of histidine-tagged proteins
od: Alireza Shariati, i wsp.
Wydane: (2023-10-01) -
Free histidine as a metal chelator in plants that accumulate nickel
od: Kramer, U, i wsp.
Wydane: (1996)