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

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 P2(1)2(1)2(1), with unit-cell parameters a = 70.2, b = 100.7, c = 132.3 Å.

SUBMITTER: Textor LC

PROVIDER: S-EPMC3232160 | biostudies-literature | 2011 Dec

REPOSITORIES: biostudies-literature

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

Textor Larissa C LC Santos Jademilson C JC Cuadrado Nazaret Hidalgo NH Roig Manuel G MG Zhadan Galina G GG Shnyrov Valery L VL Polikarpov Igor I

Acta crystallographica. Section F, Structural biology and crystallization communications 20111130 Pt 12

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 ...[more]

PMID: 22139187

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