3CQA

Crystal structure of human fibroblast growth factor-1 with mutations Glu81Ala and Lys101Ala

Summary for 3CQA

• Entry DOI: 10.2210/pdb3cqa/pdb
• Descriptor: Heparin-binding growth factor 1, SULFATE ION, FORMIC ACID, ... (4 entities in total)
• Functional Keywords: crystal packing, acetylation, angiogenesis, developmental protein, differentiation, growth factor, heparin-binding, mitogen, polymorphism, hormone
• Biological source: Homo sapiens (Human)
• Cellular location: Secreted: P05230
• Total number of polymer chains: 2
• Total formula weight: 32872.80

Authors

Meher, A.K.,Honjo, E.,Kuroki, R.,Lee, J.,Somasundaram, T.,Blaber, M. (deposition date: 2008-04-02, release date: 2009-04-07, Last modification date: 2023-08-30)

Primary citation

Meher, A.K.,Blaber, S.I.,Lee, J.,Honjo, E.,Kuroki, R.,Blaber, M.
Engineering an improved crystal contact across a solvent-mediated interface of human fibroblast growth factor 1.
Acta Crystallogr.,Sect.F, 65:1136-1140, 2009

PubMed 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.

PubMed: 19923735
DOI: 10.1107/S1744309109036987

Experimental method

X-RAY DIFFRACTION (1.8 Å)