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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, author
Blaber, Sachiko, author
Lee, Jihun, 1979-, author
Honjo, Ejiro, author
Kuroki, Ryota, author
Blaber, Michael, author
Type of Resource: text
Genre: text
Issuance: serial
Date Issued: 2009
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_migr_biomed_faculty_publications-0017 (IID)
Keywords: protein crystallization, side-chain entropy, neutron diffraction, protein engineering, crystal growth
Uncontrolled subjects: Crystallization, Crystallography, X-Ray, Fibroblast Growth Factor 1, Humans, Models, Molecular, Molecular Sequence Data, Mutagenesis, Neutron Diffraction, Protein Conformation, Protein Engineering, Solvents, X-Ray Diffraction
Note: Originally published in Acta Crystallographica. Section F, Structural Biology and Crystallization Communications.
Citation: Meher, A.K., Blaber, S.I., Lee, J., Honjo, E., Kuroki, R. and Blaber, M. (2009). Engineering an improved crystal contact across a solvent-mediated interface of human fibroblast growth factor-1. Acta Cryst. F. 65, 1136-1140.
Subject(s): Biochemistry
Biophysics
Molecular biology
Cytology
Developmental biology
Clinical biochemistry
Medical sciences
Persistent Link to This Record: http://purl.flvc.org/fsu/fd/FSU_migr_biomed_faculty_publications-0017
Owner Institution: FSU
Is Part of Series: Department of Biomedical Sciences Faculty Publications.
Is Part Of: Acta Crystallographica. Section F, Structural Biology and Crystallization Communications.
Issue: Pt 11, 65

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Meher, A., Blaber, S., 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_migr_biomed_faculty_publications-0017