title: Plasmodium falciparum ARFGAP: expression and crystallization of the catalytic domain.
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.
authors.affiliation: Division of Geographic Medicine and Center for Biophysical Sciences and Engineering, University of Alabama at Birmingham, CBSE-250, 1025 18th Street South, Birmingham, AL 35294, USA.
authors.forename: Olga
authors.initials: O
authors.lastname: Senkovich
authors.forename: Debasish
authors.initials: D
authors.lastname: Chattopadhyay
mesh_terms: D020727:ADP-Ribosylation Factors / Q000096:biosynthesis / Q000737:chemistry / Q000235:genetics*; D000818:Animals; D020134:Catalytic Domain; D003460:Crystallization; D018360:Crystallography, X-Ray; D020690:GTPase-Activating Proteins / Q000096:biosynthesis / Q000737:chemistry / Q000235:genetics*; D010963:Plasmodium falciparum / Q000737:chemistry / Q000378:metabolism*
chemical_list: D020690:GTPase-Activating Proteins; D020727:ADP-Ribosylation Factors