Polymer-Induced Heteronucleation for Protein Single Crystal Growth: Structural Elucidation of Bovine Liver Catalase and Concanavalin A Forms

Autor:	Adam J. Matzger, Leila M. Foroughi, You Na Kang
Rok vydání:	2011
Předmět:	chemistry.chemical_classification biology Chemistry Crystal growth General Chemistry Polymer Condensed Matter Physics Small molecule law.invention Crystal Crystallography Structural biology Concanavalin A law biology.protein General Materials Science Crystallization Protein crystallization
Zdroj:	Crystal Growth & Design. 11:1294-1298
ISSN:	1528-7505 1528-7483
DOI:	10.1021/cg101518f
Popis:	Obtaining single crystals for X-ray diffraction remains a major bottleneck in structural biology; when existing crystal growth methods fail to yield suitable crystals, often the target rather than the crystallization approach is reconsidered. Here we demonstrate that polymer-induced heteronucleation, a powerful technique that has been used for small molecule crystallization form discovery, can be applied to protein crystallization by optimizing the heteronucleant composition and crystallization formats for crystallizing a wide range of protein targets. Applying these advances to two benchmark proteins resulted in dramatically increased crystal size, enabling structure determination, for a half century old form of bovine liver catalase (BLC) that had previously only been characterized by electron microscopy, and the discovery of two new forms of concanavalin A (conA) from the Jack bean and accompanying structural elucidation of one of these forms.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::fd97e5f2173c3142e29eaf6294de1f70 https://doi.org/10.1021/cg101518f Zobrazit plný text záznamu