Purification, crystallization and preliminary crystallographic analysis of peroxidase from the palm tree Chamaerops excelsa

Author(s)

Textor, Larissa C. ; Santos, Jademilson C. ; Hidalgo Cuadrado, Nazaret ; Roig, Manuel G. ; Zhadan, Galina G. ; Shnyrov, Valery L. ; Polikarpov, Igor

• Document type: Journal article
• Source: ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS; v. 67, p. 4-pg., 2011-12-01.

Abstract

Plant peroxidases are presently used extensively in a wide range of biotechnological applications owing to their high environmental and thermal stability. As part of efforts towards the discovery of appealing new biotechnological enzymes, the peroxidase from leaves of the palm tree Chamaerops excelsa (CEP) was extracted, purified and crystallized in its native form. An X-ray diffraction data set was collected at a synchrotron source and data analysis showed that the CEP crystals belonged to the orthorhombic space group P212121, with unit-cell parameters a = 70.2, b = 100.7, c = 132.3 angstrom. (AU)

• FAPESP's process: 09/52840-7 - Center of Biological and Industrial Processes for Biofuels - CeProBIO
• Grantee: Igor Polikarpov
• Support Opportunities: Program for Research on Bioenergy (BIOEN) - Thematic Grants
• FAPESP's process: 08/56255-9 - Structure and function of enzymes and auxiliary proteins from Trichoderma, active in cell-wall hydrolysis
• Grantee: Igor Polikarpov
• Support Opportunities: Program for Research on Bioenergy (BIOEN) - Thematic Grants
• FAPESP's process: 09/14333-6 - Structural characterization of the peroxisome proliferator-activated receptors (PPARs) types alpha and gamma complexes and its agonists
• Grantee: Jademilson Celestino dos Santos
• Support Opportunities: Scholarships in Brazil - Doctorate (Direct)