Generation of Size-Controlled, Submicrometer Protein Crystals
Source abstract
Abstract
Cross-linked protein crystals represent a new class of micro- and mesoporous materials with properties potentially useful in technologies as diverse as chiral separations and drug delivery. These applications require the generation of protein crystals in formats and sizes quite distinct from the traditional submillimeter single crystals favored by structural biologists. Here we report a high-yield method for forming monodisperse protein crystals with tunable dimensions ranging from 250 nm up to tens of micrometers. X-ray powder diffraction of these crystallites confirms that the hen egg white lysozyme crystals are identical in structure to that of the bulk tetragonal lysozyme ( a = 79.05 Å; c = 37.96 Å).
Source: openalex_inverted_index · Quality: baseline
Research context
OpenAlex topics: Enzyme Structure and Function · Crystallization and Solubility Studies · Protein Structure and Dynamics
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Affiliations
Departments of Chemistry and Biochemistry, MS-140 Rice University, 6100 Main St, Houston, Texas 77005 and Department of Biochemistry, University of Wisconsin−Madison, Room 6607, 433 Babcock Drive, Madison, Wisconsin 53706-1544
References (30)
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