Shape-control of protein crystals in patterned microwells

Liying Wang; Hyung Lee Min; Jeremy Barton; Laura Hughes; Teri W. Odom

doi:10.1021/ja077956v

Shape-control of protein crystals in patterned microwells

Liying Wang, Hyung Lee Min, Jeremy Barton, Laura Hughes, Teri W. Odom

Northwestern University

Research output: Contribution to journal › Article

23 Citations (Scopus)

Abstract

This Communication demonstrates how selectively functionalized, patterned microscale wells can be used as small-volume (fL) crystallization vessels to grow protein crystals. This surface-patterned approach enables proteins to be crystallized with well-controlled shapes and uniform sizes from 3 μm down to 600 nm. Three different proteins - lysozyme, thaumatin, and glucose isomerase - were crystallized as model systems to demonstrate the generality of this technique. Different polymorphs were formed simply by controlling the evaporation conditions.

Original language	English
Pages (from-to)	2142-2143
Number of pages	2
Journal	Journal of the American Chemical Society
Volume	130
Issue number	7
DOIs	https://doi.org/10.1021/ja077956v
Publication status	Published - Feb 20 2008

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ASJC Scopus subject areas

Catalysis
Chemistry(all)
Biochemistry
Colloid and Surface Chemistry

Cite this

Wang, L., Min, H. L., Barton, J., Hughes, L., & Odom, T. W. (2008). Shape-control of protein crystals in patterned microwells. Journal of the American Chemical Society, 130(7), 2142-2143. https://doi.org/10.1021/ja077956v

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10.1021/ja077956v