Crystallization and heavy‐atom derivatization of StHsp14.0, a small heat‐shock protein from Sulfolobus tokodaii

Publisher: John Wiley & Sons Inc

E-ISSN: 1744-3091|65|10|1007-1010

ISSN: 1744-3091

Source: Acta Crystallographica Section F, Vol.65, Iss.10, 2009-10, pp. : 1007-1010

Disclaimer: Any content in publications that violate the sovereignty, the constitution or regulations of the PRC is not accepted or approved by CNPIEC.

Previous Menu Next

Abstract

Small heat‐shock proteins (sHsps) bind and stabilize proteins denatured by heat or other stresses in order to prevent unfavourable protein aggregation. StHsp14.0 is an sHsp found in the acidothermophilic archaeon Sulfolobus tokodaii. A variant of StHsp14.0 was crystallized by the sitting‐drop vapour‐diffusion method. The crystals diffracted X‐rays to 1.85 Å resolution and belonged to space group P21212, with unit‐cell parameters a = 40.4, b = 61.1, c = 96.1 Å. The VM value was estimated to be 2.1 Å3 Da−1, assuming the presence of two molecules in the asymmetric unit. Heavy‐atom derivative crystals were prepared successfully by the cocrystallization method and are isomorphic to native crystals.