ArticleActa crystallographica. Section D, Biological crystallography2008
High-molecular-weight polymers for protein crystallization: poly-gamma-glutamic acid-based precipitants.
Article in Acta crystallographica. Section D, Biological crystallography, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 19 citations in OpenAlex.
- Poly (γ) glutamic acid: a unique microbial biopolymer with diverse commercial applicability.Frontiers in microbiology · 2024Review
- Proline/alanine-rich sequence (PAS) polypeptides as an alternative to PEG precipitants for protein crystallization.Acta crystallographica. Section F, Structural biology communications · 2020Article
- Structure of the GH9 glucosidase/glucosaminidase from Vibrio cholerae.Acta crystallographica. Section F, Structural biology communications · 2018Article
- Structure of Rubisco from Arabidopsis thaliana in complex with 2-carboxyarabinitol-1,5-bisphosphate.Acta crystallographica. Section D, Structural biology · 2018Article
- Post-polymerization modification of poly(L-glutamic acid) with D-(+)-glucosamine.Molecules (Basel, Switzerland) · 2014Article
- Structural basis for kinesin-1:cargo recognition.Science (New York, N.Y.) · 2013Article
- Structure of Leishmania major cysteine synthase.Acta crystallographica. Section F, Structural biology and crystallization communications · 2012Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Protein crystallization has been revolutionized by the introduction of high-throughput technologies, which have led to a speeding up of the process while simultaneously reducing the amount of protein sample necessary. Nonetheless, the chemistry dimension of protein crystallization has remained relatively undeveloped. Most crystallization screens are based on the same set of precipitants. To address this shortcoming, the development of new protein precipitants based on poly-gamma-glutamic acid (PGA) polymers with different molecular-weight ranges is reported here: PGA-LM (low molecular weight) of approximately 400 kDa and PGA-HM (high molecular weight) of >1,000 kDa. It is also demonstrated that protein precipitants can be expanded further to polymers with much higher molecular weight than those that are currently in use. Furthermore, the modification of PGA-like polymers by covalent attachments of glucosamine substantially improved their solubility without affecting their crystallization properties. Some preliminary PGA-based screens are presented here.
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