Cookies on this website
We use cookies to ensure that we give you the best experience on our website. If you click 'Continue' we'll assume that you are happy to receive all cookies and you won't see this message again. Click 'Find out more' for information on how to change your cookie settings.

The neurotrophins show a high degree of amino acid sequence homology, share similar solution properties, and display distinct but parallel functionalities. Here we report the crystallization and preliminary X-ray characterization of three neurotrophins: brain-derived neurotrophin, neurotrophin 3, and the heterodimer between brain-derived neurotrophin and neurotrophin 4. These findings are related to other published crystal parameters for neurotrophins, leading to the observation that, although crystal packing is highly variant, neurotrophins share common solubilities with respect to crystal growth.

Original publication

DOI

10.1002/pro.5560050520

Type

Journal article

Journal

Protein Sci

Publication Date

05/1996

Volume

5

Pages

973 - 977

Keywords

Brain-Derived Neurotrophic Factor, Crystallization, Crystallography, X-Ray, Humans, Nerve Growth Factors, Neurotrophin 3, Protein Multimerization, Recombinant Proteins