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PDBsum entry 3crh
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References listed in PDB file
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Key reference
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Title
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Engineering an improved crystal contact across a solvent-Mediated interface of human fibroblast growth factor 1.
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Authors
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A.K.Meher,
S.I.Blaber,
J.Lee,
E.Honjo,
R.Kuroki,
M.Blaber.
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Ref.
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Acta Crystallogr Sect F Struct Biol Cryst Commun, 2009,
65,
1136-1140.
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PubMed id
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Abstract
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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.
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