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 | |
| Publication status | Published - Feb 20 2008 |
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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 journal › Article
}
TY - JOUR
T1 - Shape-control of protein crystals in patterned microwells
AU - Wang, Liying
AU - Min, Hyung Lee
AU - Barton, Jeremy
AU - Hughes, Laura
AU - Odom, Teri W
PY - 2008/2/20
Y1 - 2008/2/20
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=39549092135&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=39549092135&partnerID=8YFLogxK
U2 - 10.1021/ja077956v
DO - 10.1021/ja077956v
M3 - Article
VL - 130
SP - 2142
EP - 2143
JO - Journal of the American Chemical Society
JF - Journal of the American Chemical Society
SN - 0002-7863
IS - 7
ER -