Creation of Cross-Linked Crystals With Intermolecular Disulfide Bonds Connecting Symmetry-Related Molecules Allows Retention of Tertiary Structure in Different Solvent Conditions

Protein crystals are generally fragile and sensitive to subtle changes such as pH, ionic strength, and/or temperature in their crystallization mother liquor. Here, using T4 phage lysozyme as a model protein, the three-dimensional rigidification of protein crystals was conducted by introducing disulf...

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Detalles Bibliográficos

Principais autores:	Takeshi Hiromoto, Teikichi Ikura, Eijiro Honjo, Michael Blaber, Ryota Kuroki, Taro Tamada
Formato:	Artigo
Idioma:	Inglês
Publicado:	Frontiers Media S.A. 2022-06-01
Series:	Frontiers in Molecular Biosciences
Assuntos:	T4 phage lysozyme crystal immobilization disulfide cross-linking x-ray crystallography pH tolerance osmotic tolerance
Acceso en liña:	https://www.frontiersin.org/articles/10.3389/fmolb.2022.908394/full
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