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Publication Abstract from PubMed

Two commonly encountered bottlenecks in the structure determination of a protein by X-ray crystallography are screening for conditions that give high-quality crystals and, in the case of novel structures, finding derivatization conditions for experimental phasing. In this study, the phasing molecule 5-amino-2,4,6-triiodoisophthalic acid (I3C) was added to a random microseed matrix screen to generate high-quality crystals derivatized with I3C in a single optimization experiment. I3C, often referred to as the magic triangle, contains an aromatic ring scaffold with three bound I atoms. This approach was applied to efficiently phase the structures of hen egg-white lysozyme and the N-terminal domain of the Orf11 protein from Staphylococcus phage P68 (Orf11 NTD) using SAD phasing. The structure of Orf11 NTD suggests that it may play a role as a virion-associated lysin or endolysin.

Combining random microseed matrix screening and the magic triangle for the efficient structure solution of a potential lysin from bacteriophage P68.,Truong JQ, Panjikar S, Shearwin-Whyatt L, Bruning JB, Shearwin KE Acta Crystallogr D Struct Biol. 2019 Jul 1;75(Pt 7):670-681. doi:, 10.1107/S2059798319009008. Epub 2019 Jul 2. PMID:31282476^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.