Journal article

Publication year: 2009

Pages: 1232-1235

Journal: Acta Crystallographica. Section D: Biological Crystallography

Volume number: 65

Issue number: 11

ISSN: 2059-7983

DOI Link: https://doi.org/10.1107/S0907444909034106

Publisher: Wiley

Abstract: 
Crystallization of phytochromes and other photochromic proteins is hampered by the conformational changes that they undergo on exposure to light. As a canonical phytochrome, cyanobacterial Cph1 switches between two stable states upon absorption of red/far-red light. Consequently, it is mandatory to work in darkness from protein purification to crystal cryoprotection in order to ensure complete occupancy of one state or the other. With the simple and inexpensive methods that have been developed, phytochromes and other photochromic molecules can effectively be handled and crystallized, as has been demonstrated by the solution of the three-dimensional structure of the Cph1 sensory module.

Harvard Citation style: Mailliet, J., Psakis, G., Schroeder, C., Kaltofen, S., Durrwang, U., Hughes, J., et al. (2009) Dwelling in the dark: procedures for the crystallography of phytochromes and other photochromic proteins, Acta Crystallographica. Section D: Biological Crystallography, 65(11), pp. 1232-1235. https://doi.org/10.1107/S0907444909034106

APA Citation style: Mailliet, J., Psakis, G., Schroeder, C., Kaltofen, S., Durrwang, U., Hughes, J., & Essen, L. (2009). Dwelling in the dark: procedures for the crystallography of phytochromes and other photochromic proteins. Acta Crystallographica. Section D: Biological Crystallography. 65(11), 1232-1235. https://doi.org/10.1107/S0907444909034106