English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Plus monthly

Global: Zendy Tools annual

Global: Zendy Tools monthly

Global: Zendy Free Plan

Mechanism of crystal growth is an object to understand and control crystal size and quality. Ribonuclease A (RNaseA) is known to crystallize in the trigonal form using 3 M NaCl and 30% (NH4)2SO4 as precipitants. Crystal growth of trigonal RNaseA was investigated. Solubility curves were determined at 10, 20, and 35°C. It was found that solubility decreases at higher temperature. Negative correlation between solubility and temperature is known for hydrophobic proteins. However, RNaseA is not hydrophobic protein, and high concentration of the precipitants attributes temperature dependence of solubility curve. Crystal morphology changed from a hexagonal bipyramidal surrounded by {1 0 0} and {1 0 1} to a truncated cube surrounded by {1 0 1} with increment of concentrations of the precipitants (Fig. 1). The salt effect on crystal morphology and surface microtopograph will be discussed based on the intermolecular interactions. Besides impurity e ffec t wi l l be d i scussed , because RNaseA of commercial source includes slight amount of deamidated protein and dimeric protein.

Protein crystallization in the presence of amino acids and their derivatives. (1) The effect