ReviewActa crystallographica. Section F, Structural biology communications2015
In vivo protein crystallization in combination with highly brilliant radiation sources offers novel opportunities for the structural analysis of post-translationally modified eukaryotic proteins.
Review in Acta crystallographica. Section F, Structural biology communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 27 citations in OpenAlex.
- Review
- Crowding and in-Cell Crystallization.Sub-cellular biochemistry · 2025Review
- A snapshot love story: what serial crystallography has done and will do for us.Acta crystallographica. Section D, Structural biology · 2024Review
- Review
- Convolutional neural network approach for the automated identification ofJournal of applied crystallography · 2024Article
- Article
- Rapid screening ofJournal of applied crystallography · 2020Article
- Construction of gateway-compatible baculovirus expression vectors for high-throughput protein expression and in vivo microcrystal screening.Scientific reports · 2020Article
- Enhanced X-ray diffraction of in vivo-grown μNS crystals by viscous jets at XFELs.Acta crystallographica. Section F, Structural biology communications · 2020Article
- What is the structural chemistry of the living organism at its temperature and pressure?Acta crystallographica. Section D, Structural biology · 2020Review
- In cellulo crystallization of Trypanosoma brucei IMP dehydrogenase enables the identification of genuine co-factors.Nature communications · 2020Article
- Data-driven challenges and opportunities in crystallography.Emerging topics in life sciences · 2019Article
- Strategies for sample delivery for femtosecond crystallography.Acta crystallographica. Section D, Structural biology · 2019Review
- Microcrystallography of Protein Crystals and In Cellulo Diffraction.Journal of visualized experiments : JoVE · 2017Article
- A pipeline for structure determination of in vivo-grown crystals using in cellulo diffraction.Acta crystallographica. Section D, Structural biology · 2016Article
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
During the last decade, the number of three-dimensional structures solved by X-ray crystallography has increased dramatically. By 2014, it had crossed the landmark of 100 000 biomolecular structures deposited in the Protein Data Bank. This tremendous increase in successfully crystallized proteins is primarily owing to improvements in cloning strategies, the automation of the crystallization process and new innovative approaches to monitor crystallization. However, these improvements are mainly restricted to soluble proteins, while the crystallization and structural analysis of membrane proteins or proteins that undergo major post-translational modifications remains challenging. In addition, the need for relatively large crystals for conventional X-ray crystallography usually prevents the analysis of dynamic processes within cells. Thus, the advent of high-brilliance synchrotron and X-ray free-electron laser (XFEL) sources and the establishment of serial crystallography (SFX) have opened new avenues in structural analysis using crystals that were formerly unusable. The successful structure elucidation of cathepsin B, accomplished by the use of microcrystals obtained by in vivo crystallization in baculovirus-infected Sf9 insect cells, clearly proved that crystals grown intracellularly are very well suited for X-ray analysis. Here, methods by which in vivo crystals can be obtained, isolated and used for structural analysis by novel highly brilliant XFEL and synchrotron-radiation sources are summarized and discussed.
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