Shape-control of protein crystals in patterned microwells

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

Research output: Contribution to journalArticle

22 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 languageEnglish
Pages (from-to)2142-2143
Number of pages2
JournalJournal of the American Chemical Society
Volume130
Issue number7
DOIs
Publication statusPublished - Feb 20 2008

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Proteins
xylose isomerase
Crystals
Muramidase
Crystallization
Polymorphism
Glucose
Evaporation
Enzymes
Communication

ASJC Scopus subject areas

  • Chemistry(all)

Cite this

Shape-control of protein crystals in patterned microwells. / Wang, Liying; Min, Hyung Lee; Barton, Jeremy; Hughes, Laura; Odom, Teri W.

In: Journal of the American Chemical Society, Vol. 130, No. 7, 20.02.2008, p. 2142-2143.

Research output: Contribution to journalArticle

Wang, Liying ; Min, Hyung Lee ; Barton, Jeremy ; Hughes, Laura ; Odom, Teri W. / Shape-control of protein crystals in patterned microwells. In: Journal of the American Chemical Society. 2008 ; Vol. 130, No. 7. pp. 2142-2143.
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