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Title: Purification, crystallization and preliminary X-ray analysis of urease from pigeon pea (Cajanus cajan)

Abstract

Urease from pigeon pea was purified and crystallized and X-ray diffraction data were collected at 2.5 Å resolution. Urease is a seed protein that is common to most Leguminosae. It also occurs in many bacteria, fungi and several species of yeast. Urease catalyzes the hydrolysis of urea to ammonia and carbon dioxide, thus allowing organisms to use exogenous and internally generated urea as a nitrogen source. Urease from pigeon pea seeds has been purified to electrophoretic homogeneity using a series of steps involving ammonium sulfate fractionation, acid precipitation, ion-exchange and size-exclusion chromatography techniques. The pigeon pea urease was crystallized and the resulting crystals diffracted to 2.5 Å resolution. The crystals belong to the rhombohedral space group R32, with unit-cell parameters a = b = 176.29, c = 346.44 Å.

Authors:
;  [1]
  1. Centre of Advanced Study in Crystallography and Biophysics, University of Madras, Guindy Campus, Chennai 600 025 (India)
Publication Date:
OSTI Identifier:
22360595
Resource Type:
Journal Article
Journal Name:
Acta Crystallographica. Section F
Additional Journal Information:
Journal Volume: 64; Journal Issue: Pt 7; Other Information: PMCID: PMC2443974; PMID: 18607103; PUBLISHER-ID: hc5058; OAI: oai:pubmedcentral.nih.gov:2443974; Copyright (c) International Union of Crystallography 2008; Country of input: International Atomic Energy Agency (IAEA); Journal ID: ISSN 1744-3091
Country of Publication:
United Kingdom
Language:
English
Subject:
75 CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY; AMMONIA; AMMONIUM SULFATES; CARBON DIOXIDE; CRYSTALLIZATION; CRYSTALS; FRACTIONATION; ION EXCHANGE; NITROGEN; PRECIPITATION; RESOLUTION; SPACE GROUPS; UREA; X-RAY DIFFRACTION

Citation Formats

Balasubramanian, Anuradha, and Ponnuraj, Karthe. Purification, crystallization and preliminary X-ray analysis of urease from pigeon pea (Cajanus cajan). United Kingdom: N. p., 2008. Web. doi:10.1107/S1744309108016849.
Balasubramanian, Anuradha, & Ponnuraj, Karthe. Purification, crystallization and preliminary X-ray analysis of urease from pigeon pea (Cajanus cajan). United Kingdom. https://doi.org/10.1107/S1744309108016849
Balasubramanian, Anuradha, and Ponnuraj, Karthe. 2008. "Purification, crystallization and preliminary X-ray analysis of urease from pigeon pea (Cajanus cajan)". United Kingdom. https://doi.org/10.1107/S1744309108016849.
@article{osti_22360595,
title = {Purification, crystallization and preliminary X-ray analysis of urease from pigeon pea (Cajanus cajan)},
author = {Balasubramanian, Anuradha and Ponnuraj, Karthe},
abstractNote = {Urease from pigeon pea was purified and crystallized and X-ray diffraction data were collected at 2.5 Å resolution. Urease is a seed protein that is common to most Leguminosae. It also occurs in many bacteria, fungi and several species of yeast. Urease catalyzes the hydrolysis of urea to ammonia and carbon dioxide, thus allowing organisms to use exogenous and internally generated urea as a nitrogen source. Urease from pigeon pea seeds has been purified to electrophoretic homogeneity using a series of steps involving ammonium sulfate fractionation, acid precipitation, ion-exchange and size-exclusion chromatography techniques. The pigeon pea urease was crystallized and the resulting crystals diffracted to 2.5 Å resolution. The crystals belong to the rhombohedral space group R32, with unit-cell parameters a = b = 176.29, c = 346.44 Å.},
doi = {10.1107/S1744309108016849},
url = {https://www.osti.gov/biblio/22360595}, journal = {Acta Crystallographica. Section F},
issn = {1744-3091},
number = Pt 7,
volume = 64,
place = {United Kingdom},
year = {2008},
month = {7}
}