Skip to Content
Merck
  • Crystallization and heavy-atom derivatization of StHsp14.0, a small heat-shock protein from Sulfolobus tokodaii.

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

Acta crystallographica. Section F, Structural biology and crystallization communications (2009-10-24)
Takuro Hayashi, Tetsuya Abe, Kazuki Takeda, Nobuhiko Akiyama, Masafumi Yohda, Kunio Miki
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 A resolution and belonged to space group P2(1)2(1)2, with unit-cell parameters a = 40.4, b = 61.1, c = 96.1 A. The V(M) value was estimated to be 2.1 A(3) 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.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
Rubidium chloride, ReagentPlus®, ≥99.0% (metals basis)
Sigma-Aldrich
Rubidium chloride, BioUltra, for molecular biology, ≥99.0% (AT)
Sigma-Aldrich
Rubidium chloride, 99.8% trace metals basis
Sigma-Aldrich
Rubidium chloride, 99.95% trace metals basis