Protein-macrocycle polymorphism: crystal form IV of the Ralstonia solanacearum lectin-sulfonato-calix[8]arene complex.

Autor: Mockler NM; School of Biological and Chemical Sciences, University of Galway, University Road, Galway H91 TK33, Ireland., Ramberg KO; School of Biological and Chemical Sciences, University of Galway, University Road, Galway H91 TK33, Ireland., Crowley PB; School of Biological and Chemical Sciences, University of Galway, University Road, Galway H91 TK33, Ireland.
Jazyk: angličtina
Zdroj: Acta crystallographica. Section D, Structural biology [Acta Crystallogr D Struct Biol] 2023 Jul 01; Vol. 79 (Pt 7), pp. 624-631. Date of Electronic Publication: 2023 Jun 14.
DOI: 10.1107/S2059798323003832
Abstrakt: Controlled protein assembly and crystallization is necessary as a means of generating diffraction-quality crystals as well as providing a basis for new types of biomaterials. Water-soluble calixarenes are useful mediators of protein crystallization. Recently, it was demonstrated that Ralstonia solanacearum lectin (RSL) co-crystallizes with anionic sulfonato-calix[8]arene (sclx 8 ) in three space groups. Two of these co-crystals only grow at pH ≤ 4 where the protein is cationic, and the crystal packing is dominated by the calixarene. This paper describes a fourth RSL-sclx 8 co-crystal, which was discovered while working with a cation-enriched mutant. Crystal form IV grows at high ionic strength in the pH range 5-6. While possessing some features in common with the previous forms, the new structure reveals alternative calixarene binding modes. The occurrence of C 2 -symmetric assemblies, with the calixarene at special positions, appears to be an important result for framework fabrication. Questions arise regarding crystal screening and exhaustive searching for polymorphs.
(open access.)
Databáze: MEDLINE
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