Literature DB >> 15063323

Plasmodium falciparum ARFGAP: expression and crystallization of the catalytic domain.

Olga Senkovich1, Debasish Chattopadhyay.   

Abstract

GTPase activating protein for ARF GTPAse (ARFGAP) from the malaria parasite Plasmodium falciparum was expressed, purified and crystallized. Crystals of ARFGAP belong to trigonal space group P321 (or its enantiomorph) with unit cell parameters a=b=95.89 and c=92.46 A. Diffraction data to 2.4-A resolution have been collected. Calculation of self-rotation function suggested the presence of two molecules in the asymmetric unit.

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Year:  2004        PMID: 15063323     DOI: 10.1016/j.bbapap.2003.10.007

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  3 in total

1.  Structure of Plasmodium falciparum ADP-ribosylation factor 1.

Authors:  William J Cook; Craig D Smith; Olga Senkovich; Anthony A Holder; Debasish Chattopadhyay
Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun       Date:  2010-10-27

2.  Structure of the catalytic domain of Plasmodium falciparum ARF GTPase-activating protein (ARFGAP).

Authors:  William J Cook; Olga Senkovich; Debasish Chattopadhyay
Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun       Date:  2011-10-25

3.  Recombinant protein of Haemonchus contortus small GTPase ADP-ribosylation factor 1 (HcARF1) modulate the cell mediated immune response in vitro.

Authors:  Javaid Ali Gadahi; Muhammad Ehsan; Shuai Wang; Zhenchao Zhang; Ruofeng Yan; Xiaokai Song; Lixin Xu; Xiangrui Li
Journal:  Oncotarget       Date:  2017-11-26
  3 in total

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