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. 1975 Jan;72(1):398–399. doi: 10.1073/pnas.72.1.398

Crystallization and Crystal Data of Monellin

Alexander Wlodawer 1, Keith O Hodgson 1
PMCID: PMC432313  PMID: 16592216

Abstract

Crystals of monellin, a sweet protein from Dioscoreophyllum cumminsii, were grown by vapor diffusion of 20% ethanol into buffered protein solution. The crystals are orthorhombic, belonging to space group P21212, with a = 54.4 Å, b = 113.0 Å, c = 40.8 Å, and V = 250,300 Å3. The asymmetric unit contains two complete molecules of monellin. The diffraction pattern of this crystal form extends to at least 2.5 Å, indicating that x-ray structural analysis is possible to near-atomic resolution.

Keywords: sweet protein, x-ray diffraction, vapor diffusion

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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