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Crystallography's Grail found in PNAS?

Researchers have, since 1988, been searching for a so-called "universal nucleant," that is, a material that will nucleate crystal formation, much as a grain of sand nucleates the formation of a pearl. Buried in the biophysics section of PNAS's January 6 Early Edition is linkurl:a somewhat esoteric paper;http://www.pnas.org/cgi/content/abstract/0504860102v1 that may just end this search -- and open one of structural biology's most persistent bottlenecks, generating high-quality crysta

By | January 10, 2006

Researchers have, since 1988, been searching for a so-called "universal nucleant," that is, a material that will nucleate crystal formation, much as a grain of sand nucleates the formation of a pearl. Buried in the biophysics section of PNAS's January 6 Early Edition is linkurl:a somewhat esoteric paper;http://www.pnas.org/cgi/content/abstract/0504860102v1 that may just end this search -- and open one of structural biology's most persistent bottlenecks, generating high-quality crystals for x-ray crystallography, in the bargain. "Nucleation is the crucial step that determines the entire crystallization process. Hence, the holy grail is to design a 'universal nucleant,' a substrate that induces the nucleation of crystals of any protein," Naomi Chayen and Emmanuel Saridakis, of Imperial College London, and Richard Sear, of the University of Surrey, write. The trio theorize that "mesoporous materials" -- that is, substrates with pores of varying diameters -- are likely to be most generally effective at nucleating protein crystallization. The idea is that the pores can trap individual protein molecules, allowing them to seed crystallization events. And because the pores are of varying sizes, the material will be able to nucleate crystallization of a wide range of proteins. The group proves their theory experimentally, using a "bioactive gel-glass" material with pore sizes ranging from two to 10 nm in diameter to nucleate crystals of seven different proteins. According to a press release from Imperial College announcing the publication, the material "induced the crystallisation of the largest number of proteins ever crystallised using a single nucleant." That's potentially huge news for crystallographers. Obtaining high quality crystals can be a long, arduous, and reagent-intensive process involving hundreds of different permutations of concentration, precipitant, nucleant, buffer, pH, and so on. Experience is only of limited use in such studies, as what works for one protein will not necessarily work for another. So have Chayen et al. found the Grail? Perhaps. Though she doesn't include this information in her paper, Chayen tells me that the crystals are diffraction-grade. Imperial has patented the invention, and spun out a company called linkurl:Nanonucleant;http://www.nanonucleant.co.uk to commercialize it.
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