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Molecular replacement with pseudosymmetry and model dissimilarity: a case study.

Mariusz Jaskólski·Mi Li·Gary Laco·Alla Gustchina·Alexander Wlodawer
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Abstract

Crystals of human T-cell leukemia virus protease (HTLV-1 PR) have been very difficult to prepare and only native data extending to 2.6 angstroms resolution could be collected. Initial attempts to solve the structure with a variety of low-sequence-identity models utilizing proteases from other retroviruses and using a number of molecular-replacement programs were unsuccessful. The structure was finally solved using Phaser, revealing extensive pseudosymmetry and significant deviations from the starting models, features that were likely to be responsible for the initial failures. The steps taken to solve this structure and some of its intriguing crystallographic aspects are discussed.

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Aspartic Acid EndopeptidasesCrystallography, X-RayHumansModels, MolecularProtease InhibitorsProtein Structure, TertiaryJournal ArticleResearch Support, N.I.H., ExtramuralResearch Support, N.I.H., IntramuralResearch Support, Non-U.S. Gov'tResearch Support, U.S. Gov't, Non-P.H.S.

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Mariusz Jaskólski, Mi Li, Gary Laco, Alla Gustchina, Alexander Wlodawer. 2006-01-18. Molecular replacement with pseudosymmetry and model dissimilarity: a case study.. https://doi.org/10.1107/s0907444905040655

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