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Cloning, Purification, Crystallization and Preliminary X-ray Crystallographic Analysis of a Cyclophilin A-like Protein From Piriformospora Indica

Cloning, Purification, Crystallization and Preliminary X-ray Crystallographic Analysis of a Cyclophilin A-like Protein From Piriformospora Indica

Harshesh Bhatt, Dipesh Kumar Trivedi, Ravi Kant Pal, Atul Kumar Johri, Narendra Tuteja, Neel Sarovar Bhavesh

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Jun 1;68(Pt 6):709-12.

PMID: 22684077

Abstract:

Cyclophilins are widely distributed both in eukaryotes and prokaryotes and have a primary role as peptidyl-prolyl cis-trans isomerases (PPIases). This study focuses on the cloning, expression, purification and crystallization of a salinity-stress-induced cyclophilin A (CypA) homologue from the symbiotic fungus Piriformospora indica. Crystallization experiments in the presence of 56 mM sodium phosphate monobasic monohydrate, 1.34 M potassium phosphate dibasic pH 8.2 yielded crystals that were suitable for X-ray diffraction analysis. The crystals belonged to the orthorhombic space group C222(1), with unit-cell parameters a = 121.15, b = 144.12, c = 110.63 Å. The crystals diffracted to a resolution limit of 2.0 Å. Analysis of the diffraction data indicated the presence of three molecules of the protein per asymmetric unit (V(M) = 4.48 Å(3) Da(-1), 72.6% solvent content).

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP10049215	Sodium phosphate monobasic monohydrate		10049-21-5	Price
AP7758114-A	Potassium phosphate dibasic		7758-11-4	Price

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