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Salt-induced aggregation of lysozyme: Implications for crystal growthCrystallization of proteins is a prerequisite for structural analysis by x-ray crystallography. While improvements in protein crystals have been obtained in microgravity onboard the U.S. Space Shuttle, attempts to improve the crystal growth process both on the ground and in space have been limited by our lack of understanding of the mechanisms involved. Almost all proteins are crystallized with the aid of a precipitating agent. Many of the common precipitating agents are inorganic salts. An understanding of the role of salts on the aggregation of protein monomers is the key to the elucidation of the mechanisms involved in protein crystallization. In order for crystallization to occur individual molecules must self-associate into aggregates. Detection and characterization of aggregates in supersaturated protein solutions is the first step in understanding salt-induced crystallization.
Document ID
19950012600
Acquisition Source
Legacy CDMS
Document Type
Conference Paper
Authors
Wilson, Lori J.
(State Univ. of East Tennessee Johnson City, TN, United States)
Date Acquired
September 6, 2013
Publication Date
October 1, 1994
Publication Information
Publication: Alabama Univ., Research Reports: 1994 NASA(ASEE Summer Faculty Fellowship Program
Subject Category
Solid-State Physics
Accession Number
95N19015
Distribution Limits
Public
Copyright
Work of the US Gov. Public Use Permitted.
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