Grießl M, Jungkunz I, Sonnewald U, Muller Y (2012)
Publication Status: Published
Publication Type: Journal article
Publication year: 2012
Publisher: WILEY-BLACKWELL
Book Volume: 68
Pages Range: 236-239
DOI: 10.1107/S1744309111055928
Chaperones promote many different molecular processes, including the folding, targeting and degradation of proteins. The best-studied chaperone system consists of the Hsp70s and their co-chaperones the Hsp40s. Chaperone function can be hijacked by viruses in plants. Potato virus Y interacts via its coat protein with an Hsp40 from Nicotiana tabacum, referred to as NtCPIP1, in order similar to to regulate replication. To understand the molecular determinants of this similar to mechanism, different variants of NtCPIP1 were expressed, purified and crystallized. While crystals of wild-type NtCPIP1 diffracted to 8.0 angstrom resolution, the deletion mutant NtCPIP1-(1:127) crystallized in space group P21212 and diffracted to 2.4 angstrom resolution.
APA:
Grießl, M., Jungkunz, I., Sonnewald, U., & Muller, Y. (2012). Purification, crystallization and preliminary X-ray diffraction analysis of the Hsp40 protein CPIP1 from Nicotiana tabacum. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 68, 236-239. https://dx.doi.org/10.1107/S1744309111055928
MLA:
Grießl, Martin, et al. "Purification, crystallization and preliminary X-ray diffraction analysis of the Hsp40 protein CPIP1 from Nicotiana tabacum." Acta Crystallographica Section F: Structural Biology and Crystallization Communications 68 (2012): 236-239.
BibTeX: Download