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

Title: Engineering an improved crystal contact across a solvent-mediated interface of human fibroblast growth factor 1.
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Name(s): Meher, Akshaya K, author
Blaber, Sachiko I, author
Lee, Jihun, author
Honjo, Ejiro, author
Kuroki, Ryota, author
Blaber, Michael, author
Type of Resource: text
Genre: journal article
text
Date Issued: 2009-11-01
Physical Form: computer
Physical Form: online resource
Extent: 1 online resource
Language(s): English
Abstract/Description: 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.
Identifier: FSU_pmch_19923735 (IID), 10.1107/S1744309109036987 (DOI), PMC2777043 (PMCID), 19923735 (RID), 19923735 (EID), S1744309109036987 (PII)
Publication Note: This NIH-funded author manuscript originally appeared in PubMed Central at https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2777043.
Subject(s): Crystallization/methods
Crystallography, X-Ray
Fibroblast Growth Factor 1/chemistry
Fibroblast Growth Factor 1/genetics
Humans
Models, Molecular
Molecular Sequence Data
Mutagenesis
Neutron Diffraction
Protein Conformation
Protein Engineering/methods
Solvents/chemistry
X-Ray Diffraction
Persistent Link to This Record: http://purl.flvc.org/fsu/fd/FSU_pmch_19923735
Owner Institution: FSU
Is Part Of: Acta crystallographica. Section F, Structural biology and crystallization communications.
1744-3091
Issue: iss. Pt 11, vol. 65

Choose the citation style.
Meher, A. K., Blaber, S. I., Lee, J., Honjo, E., Kuroki, R., & Blaber, M. (2009). Engineering an improved crystal contact across a solvent-mediated interface of human fibroblast growth factor 1. Acta Crystallographica. Section F, Structural Biology And Crystallization Communications. Retrieved from http://purl.flvc.org/fsu/fd/FSU_pmch_19923735