Crystallization, data collection and phasing of infestin 4, a factor XIIa inhibitor

Crystallization, data collection and phasing of infestin 4, a factor XIIa inhibitor

Author Campos, ITN Google Scholar
Guimaraes, B. G. Google Scholar
Medrano, F. J. Google Scholar
Tanaka, A. S. Google Scholar
Barbosa, JARG Google Scholar
Institution Ctr Biol Mol Estrutural CeBiMe
Universidade Federal de São Paulo (UNIFESP)
Abstract Infestin is a protein from Triatoma infestans (kissing bug) composed of seven Kazal-type domains that is further processed to yield several serine protease inhibitors with varying specificities. Infestins 3 and 4 are the last two domains of the infestin gene and are found in vivo in the insect's anterior midgut. the last domain, infestin 4, has been cloned, expressed and purified. Here, the crystallization of infestin 4 using the sitting-drop vapour-diffusion method with PEG 8000 as precipitant is described. Crystals belong to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a=25.89, b=45.64, c=57.41 Angstrom. X-ray diffraction data were collected to a maximum resolution of 1.8 Angstrom using a synchrotron-radiation source. Initial phases were calculated by molecular replacement using an edited rhodniin molecule as the search model. Structure refinement is in progress.
Language English
Date 2004-11-01
Published in Acta Crystallographica Section D-biological Crystallography. Copenhagen: Blackwell Munksgaard, v. 60, p. 2051-2053, 2004.
ISSN 0907-4449 (Sherpa/Romeo, impact factor)
Publisher Blackwell Munksgaard
Extent 2051-2053
Access rights Closed access
Type Article
Web of Science ID WOS:000224595200027

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