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Control of nucleation of protein crystals
Author(s) -
Blow D.M.,
Chayen N.E.,
Lloyd L.F.,
Saridakis E.
Publication year - 1994
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.5560031003
Subject(s) - nucleation , homogeneous , protein crystallization , crystallography , materials science , serial dilution , chemistry , chemical engineering , chemical physics , thermodynamics , organic chemistry , crystallization , physics , pathology , engineering , medicine , alternative medicine
Control of nucleation may be needed to obtain a reliable supply of large protein crystals, when standard techniques give many small or twinned crystals. Heterogeneous nucleation may be controlled by the use of fine filters, with the elimination of airborne contaminants by working under paraffin oil. The area of contact with the supporting vessel also has an important effect. A heterogeneous nucleant for lysozyme (identified earlier) has been shown to be effective for carboxypeptidase G 2 . Control of homogeneous nucleation (previously demonstrated by dilutions of a nucleating sample after various times of incubation) may also be achieved by incubating a sample at 1 temperature, where nucleation can occur, and changing the temperature to conditions where there is growth but no nucleation.