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Title: Crystallization and preliminary X-ray analysis of cryptolepain, a novel glycosylated serine protease from Cryptolepis buchanani

Abstract

Cryptolepain is a stable glycosylated novel serine protease was crystallized by hanging-drop method. Crystal data was processed up to 2.25 Å with acceptable statistics and structure determination of the enzyme is under way. Cryptolepain is a stable glycosylated novel serine protease purified from the latex of the medicinally important plant Cryptolepis buchanani. The molecular weight of the enzyme is 50.5 kDa, as determined by mass spectrometry. The sequence of the first 15 N-terminal resides of the protease showed little homology with those of other plant serine proteases, suggesting it to be structurally unique. Thus, it is of interest to solve the structure of the enzyme in order to better understand its structure–function relationship. X-ray diffraction data were collected from a crystal of cryptolepain and processed to 2.25 Å with acceptable statistics. The crystals belong to the orthorhombic space group C222{sub 1}, with unit-cell parameters a = 81.78, b = 108.15, c = 119.86 Å. The Matthews coefficient was 2.62 Å{sup 3} Da{sup −1} with one molecule in the asymmetric unit. The solvent content was found to be 53%. Structure determination of the enzyme is under way.

Authors:
 [1];  [2];  [1]
  1. Molecular Biology Unit, Institute of Medical Sciences, Banaras Hindu University, Varanasi 221005 (India)
  2. Department of Biotechnology, Indian Institute of Technology, Guwahati 781039, Assam (India)
Publication Date:
OSTI Identifier:
22360269
Resource Type:
Journal Article
Resource Relation:
Journal Name: Acta Crystallographica. Section F; Journal Volume: 63; Journal Issue: Pt 2; Other Information: PMCID: PMC2330135; PMID: 17277443; PUBLISHER-ID: pu5168; OAI: oai:pubmedcentral.nih.gov:2330135; Copyright (c) International Union of Crystallography 2007; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
United Kingdom
Language:
English
Subject:
75 CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY; CRYSTALLIZATION; CRYSTALS; LATEX; MASS SPECTROSCOPY; MOLECULAR WEIGHT; MOLECULES; SOLVENTS; SPACE GROUPS; X-RAY DIFFRACTION

Citation Formats

Pande, Monu, Dubey, Vikash K., and Jagannadham, Medicherla V., E-mail: vdubey@iitg.ernet.in. Crystallization and preliminary X-ray analysis of cryptolepain, a novel glycosylated serine protease from Cryptolepis buchanani. United Kingdom: N. p., 2007. Web. doi:10.1107/S1744309106054807.
Pande, Monu, Dubey, Vikash K., & Jagannadham, Medicherla V., E-mail: vdubey@iitg.ernet.in. Crystallization and preliminary X-ray analysis of cryptolepain, a novel glycosylated serine protease from Cryptolepis buchanani. United Kingdom. doi:10.1107/S1744309106054807.
Pande, Monu, Dubey, Vikash K., and Jagannadham, Medicherla V., E-mail: vdubey@iitg.ernet.in. Thu . "Crystallization and preliminary X-ray analysis of cryptolepain, a novel glycosylated serine protease from Cryptolepis buchanani". United Kingdom. doi:10.1107/S1744309106054807.
@article{osti_22360269,
title = {Crystallization and preliminary X-ray analysis of cryptolepain, a novel glycosylated serine protease from Cryptolepis buchanani},
author = {Pande, Monu and Dubey, Vikash K. and Jagannadham, Medicherla V., E-mail: vdubey@iitg.ernet.in},
abstractNote = {Cryptolepain is a stable glycosylated novel serine protease was crystallized by hanging-drop method. Crystal data was processed up to 2.25 Å with acceptable statistics and structure determination of the enzyme is under way. Cryptolepain is a stable glycosylated novel serine protease purified from the latex of the medicinally important plant Cryptolepis buchanani. The molecular weight of the enzyme is 50.5 kDa, as determined by mass spectrometry. The sequence of the first 15 N-terminal resides of the protease showed little homology with those of other plant serine proteases, suggesting it to be structurally unique. Thus, it is of interest to solve the structure of the enzyme in order to better understand its structure–function relationship. X-ray diffraction data were collected from a crystal of cryptolepain and processed to 2.25 Å with acceptable statistics. The crystals belong to the orthorhombic space group C222{sub 1}, with unit-cell parameters a = 81.78, b = 108.15, c = 119.86 Å. The Matthews coefficient was 2.62 Å{sup 3} Da{sup −1} with one molecule in the asymmetric unit. The solvent content was found to be 53%. Structure determination of the enzyme is under way.},
doi = {10.1107/S1744309106054807},
journal = {Acta Crystallographica. Section F},
number = Pt 2,
volume = 63,
place = {United Kingdom},
year = {Thu Feb 01 00:00:00 EST 2007},
month = {Thu Feb 01 00:00:00 EST 2007}
}
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