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The Protein Maker: an automated system for high-throughput parallel purification.


ABSTRACT: The Protein Maker is an automated purification system developed by Emerald BioSystems for high-throughput parallel purification of proteins and antibodies. This instrument allows multiple load, wash and elution buffers to be used in parallel along independent lines for up to 24 individual samples. To demonstrate its utility, its use in the purification of five recombinant PB2 C-terminal domains from various subtypes of the influenza A virus is described. Three of these constructs crystallized and one diffracted X-rays to sufficient resolution for structure determination and deposition in the Protein Data Bank. Methods for screening lysis buffers for a cytochrome P450 from a pathogenic fungus prior to upscaling expression and purification are also described. The Protein Maker has become a valuable asset within the Seattle Structural Genomics Center for Infectious Disease (SSGCID) and hence is a potentially valuable tool for a variety of high-throughput protein-purification applications.

SUBMITTER: Smith ER 

PROVIDER: S-EPMC3169395 | biostudies-literature | 2011 Sep

REPOSITORIES: biostudies-literature

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The Protein Maker: an automated system for high-throughput parallel purification.

Smith Eric R ER   Begley Darren W DW   Anderson Vanessa V   Raymond Amy C AC   Haffner Taryn E TE   Robinson John I JI   Edwards Thomas E TE   Duncan Natalie N   Gerdts Cory J CJ   Mixon Mark B MB   Nollert Peter P   Staker Bart L BL   Stewart Lance J LJ  

Acta crystallographica. Section F, Structural biology and crystallization communications 20110813 Pt 9


The Protein Maker is an automated purification system developed by Emerald BioSystems for high-throughput parallel purification of proteins and antibodies. This instrument allows multiple load, wash and elution buffers to be used in parallel along independent lines for up to 24 individual samples. To demonstrate its utility, its use in the purification of five recombinant PB2 C-terminal domains from various subtypes of the influenza A virus is described. Three of these constructs crystallized an  ...[more]

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