ArticlePloS one2011
Towards protein crystallization as a process step in downstream processing of therapeutic antibodies: screening and optimization at microbatch scale.
Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
7 citing papers in PubMed, 61 citations in OpenAlex.
- Advances in Downstream Processing of Monoclonal Antibodies.Antibodies (Basel, Switzerland) · 2026Review
- Phase Diagrams as a DOE Tool in Biomolecular Crystallization.Advances in biochemical engineering/biotechnology · 2026Review
- A workflow for the development of template-assisted membrane crystallization downstream processing for monoclonal antibody purification.Nature protocols · 2023Review
- Calibration-free PAT: Locating selective crystallization or precipitation sweet spot in screenings with multi-way PARAFAC models.Frontiers in bioengineering and biotechnology · 2022Article
- Downstream process development strategies for effective bioprocesses: Trends, progress, and combinatorial approaches.Engineering in life sciences · 2017Article
- Continuous Crystallization of Proteins in a Tubular Plug-Flow Crystallizer.Crystal growth & design · 2015Article
- Recent advances in technology supporting biopharmaceutical production from mammalian cells.Applied microbiology and biotechnology · 2012Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Crystallization conditions of an intact monoclonal IgG4 (immunoglobulin G, subclass 4) antibody were established in vapor diffusion mode by sparse matrix screening and subsequent optimization. The procedure was transferred to microbatch conditions and a phase diagram was built showing surprisingly low solubility of the antibody at equilibrium. With up-scaling to process scale in mind, purification efficiency of the crystallization step was investigated. Added model protein contaminants were excluded from the crystals to more than 95%. No measurable loss of Fc-binding activity was observed in the crystallized and redissolved antibody. Conditions could be adapted to crystallize the antibody directly from concentrated and diafiltrated cell culture supernatant, showing purification efficiency similar to that of Protein A chromatography. We conclude that crystallization has the potential to be included in downstream processing as a low-cost purification or formulation step.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.