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PDBsum entry 3crh

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Top Page protein ligands Protein-protein interface(s) links
Hormone PDB id
3crh
Contents
Protein chains
142 a.a.
Ligands
SO4 ×5
Waters ×108

References listed in PDB file
Key reference
Title Engineering an improved crystal contact across a solvent-Mediated interface of human fibroblast growth factor 1.
Authors A.K.Meher, S.I.Blaber, J.Lee, E.Honjo, R.Kuroki, M.Blaber.
Ref. Acta Crystallogr Sect F Struct Biol Cryst Commun, 2009, 65, 1136-1140.
PubMed id 19923735
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.
PROCHECK
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 Headers

 

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