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Crystallization and preliminary X-ray analysis of cyclophilin from Leishmania donovani

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Title Crystallization and preliminary X-ray analysis of
cyclophilin from Leishmania donovani
 
Creator Banerjee, Rahul
Dutta, Madhuri
Sen, Malabika
Datta, Alok K
 
Subject Structural Biology & Bioinformatics
 
Description Cyclophilin from the parasite Leishmania donovani is a protein with
peptidylprolyl cis±trans isomerase activity, in addition to being a
receptor for the drug cyclosporin. Crystals of the enzyme have been
obtained in space group P43212, with unit-cell parameters a = b = 48.73,
c = 140.93 A Ê , and diffract to 3.5 A Ê resolution. One molecule per
asymmetric unit gives a solvent content and Matthews coef®cient of
46% and 2.3 A Ê 3 Da
ÿ1, respectively. Molecular-replacement calculations
with human cyclophilin A as the search model give an
unambiguous solution in rotation and translation functions.
 
Date 2002
 
Type Article
PeerReviewed
 
Format application/pdf
 
Identifier http://www.eprints.iicb.res.in/742/1/ACTA_CRYSTALLOGRAPHICA_SECTION_D%2DBIOLOGICAL_CRYSTALLOGRAPHY__58(_2)_1846%2D1847;2002[23].pdf
Banerjee, Rahul and Dutta, Madhuri and Sen, Malabika and Datta, Alok K (2002) Crystallization and preliminary X-ray analysis of cyclophilin from Leishmania donovani. Acta Crystallographica Section D-Biological Crystallography, 58 (2). pp. 1846-1847.
 
Relation http://dx.doi.org/10.1107/S0907444902012611
http://www.eprints.iicb.res.in/742/