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Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Nov 1;65(Pt 11):1136-40. doi: 10.1107/S1744309109036987. Epub 2009 Oct 30.

Engineering an improved crystal contact across a solvent-mediated interface of human fibroblast growth factor 1.

Author information

1
Department of Biomedical Sciences, Florida State University, Tallahassee, 32306-4300, USA.

Abstract

Large-volume protein crystals are a prerequisite for neutron diffraction studies and their production represents a bottleneck in obtaining neutron structures. Many protein crystals that permit the collection of high-resolution X-ray diffraction data are inappropriate for neutron diffraction owing to a plate-type morphology that limits the crystal volume. Human fibroblast growth factor 1 crystallizes in a plate morphology that yields atomic resolution X-ray diffraction data but has insufficient volume for neutron diffraction. The thin physical dimension has been identified as corresponding to the b cell edge and the X-ray structure identified a solvent-mediated crystal contact adjacent to position Glu81 that was hypothesized to limit efficient crystal growth in this dimension. In this report, a series of mutations at this crystal contact designed to both reduce side-chain entropy and replace the solvent-mediated interface with direct side-chain contacts are reported. The results suggest that improved crystal growth is achieved upon the introduction of direct crystal contacts, while little improvement is observed with side-chain entropy-reducing mutations alone.

PMID:
19923735
PMCID:
PMC2777043
DOI:
10.1107/S1744309109036987
[Indexed for MEDLINE]
Free PMC Article

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