| Full text | |
| Author(s): |
Guimarães, B. G.
;
Medrano, F. J.
;
Tanaka, Aparecida Sadae
;
Barbosa, J. A. R. G.
Total Authors: 4
|
| Document type: | Journal article |
| Source: | ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY; v. 60, n. 11, p. 2051-2053, Nov. 2004. |
| Field of knowledge: | Biological Sciences - Biochemistry |
| 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 P212121, with unit-cell parameters a = 25.89, b = 45.64, c = 57.41 Å. X-ray diffraction data were collected to a maximum resolution of 1.8 Å 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. (AU) | |
| FAPESP's process: | 01/07535-0 - Structural genomics |
| Grantee: | Sergio Schenkman |
| Support Opportunities: | Regular Research Grants |