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ABSTRACT: Many Gram-negative bacteria are characterized by hair-like proteinaceous appendages on their surface known as fimbriae. In uropathogenic strains of Escherichia coli, fimbriae mediate attachment by binding to receptors on the host cell, often contributing to virulence and disease. E. coli PapD-like protein (EcpD) is a periplasmic chaperone that plays an important role in the proper folding and guiding of Yad fimbrial proteins to the outer membrane usher protein in a process known as pilus biogenesis. EcpD is essential for pilus biogenesis in uropathogenic E. coli and plays an important role in virulence. In the present study, EcpD was cloned, overexpressed, purified and crystallized by the hanging-drop vapour-diffusion method. The crystals diffracted to 1.67 Å resolution and belonged to the orthorhombic space group C222(1), with unit-cell parameters a = 100.3, b = 127.6, c = 45.9 Å. There was a single molecule in the asymmetric unit and the corresponding Matthews coefficient was calculated to be 3.02 Å(3) Da(-1), with 59% solvent content. Initial phases were determined by molecular replacement.
Acta Crystallographica Section F Structural Biology and Crystallization Communications 08/2012; 68(Pt 8):954-7. · 0.51 Impact Factor
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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 salinitystress-
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 C2221, with unit-cell
parameters a = 121.15, b = 144.12, c = 110.63 A ° . The crystals diffracted to a
resolution limit of 2.0 A ° . Analysis of the diffraction data indicated the presence
of three molecules of the protein per asymmetric unit (VM = 4.48 A ° 3 Da�1,
72.6% solvent content).
Acta Crystallographica Section F Structural Biology and Crystallization Communications 06/2012; · 0.51 Impact Factor
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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).
Acta Crystallographica Section F Structural Biology and Crystallization Communications 06/2012; 68(Pt 6):709-12. · 0.51 Impact Factor
