ArticleNature protocols2018
High-throughput in situ X-ray screening of and data collection from protein crystals at room temperature and under cryogenic conditions.
Article in Nature protocols, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 56 citations in OpenAlex.
- A user-friendly goniometer-compatible fixed-target platform for macromolecular crystallography at synchrotrons.Journal of applied crystallography · 2026Article
- Advances in Crystallography and Cryo-Electron Microscopy for the Study of Membrane Proteins.Advances in experimental medicine and biology · 2026Review
- Other Techniques.Advances in biochemical engineering/biotechnology · 2026Review
- Effects of Membrane Cholesterol on the Structure and Function of Selected Class A GPCRs─Challenges and Future Perspectives.Biochemistry · 2025Review
- Evolution of macromolecular crystallography beamlines at the Swiss Light Source and SwissFEL.Journal of synchrotron radiation · 2025Article
- YOLO-PBESW: A Lightweight Deep Learning Model for the Efficient Identification of Indomethacin Crystal Morphologies in Microfluidic Droplets.Micromachines · 2024Article
- G Protein-Coupled Receptor-Ligand Pose and Functional Class Prediction.International journal of molecular sciences · 2024Article
- Dynamic three-dimensional structures of a metal-organic framework captured with femtosecond serial crystallography.Nature chemistry · 2024Article
- Molecular Biophysics of Class A G Protein Coupled Receptors-Lipids Interactome at a Glance-Highlights from the ABiomolecules · 2023Review
- A simple goniometer-compatible flow cell for serial synchrotron X-ray crystallography.Journal of applied crystallography · 2023Article
- Microfluidic rotating-target device capable of three-degrees-of-freedom motion for efficient in situ serial synchrotron crystallography.Journal of synchrotron radiation · 2023Article
- Perspective: Structure determination of protein-ligand complexes at room temperature using X-ray diffraction approaches.Frontiers in molecular biosciences · 2023Article
- Systematic analyses of the sequence conservation and ligand interaction patterns of purinergic P1 and P2Y receptors provide a structural basis for receptor selectivity.Computational and structural biotechnology journal · 2023Article
- xia2.multiplex: a multi-crystal data-analysis pipeline.Acta crystallographica. Section D, Structural biology · 2022Article
- Quinone binding sites of cyt bc complexes analysed by X-ray crystallography and cryogenic electron microscopy.Biochemical Society transactions · 2022Review
- International Union of Basic and Clinical Pharmacology. CXII: Adenosine Receptors: A Further Update.Pharmacological reviews · 2022Review
- Molecular Simulations and Drug Discovery of Adenosine Receptors.Molecules (Basel, Switzerland) · 2022Review
- Implementation of wedged-serial protein crystallography at PROXIMA-1.Journal of synchrotron radiation · 2022Article
- Integrated sample-handling and mounting system for fixed-target serial synchrotron crystallography.Acta crystallographica. Section D, Structural biology · 2021Article
- Purinergic GPCR transmembrane residues involved in ligand recognition and dimerization.Methods in cell biology · 2021Review
Corrections and comments
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Authors and funding
13 authors at 3 institutions in 2 countries.
Funding
Abstract
Protein crystallography has significantly advanced in recent years, with in situ data collection, in which crystals are placed in the X-ray beam within their growth medium, being a major point of focus. In situ methods eliminate the need to harvest crystals, a previously unavoidable drawback, particularly for often small membrane-protein crystals. Here, we present a protocol for the high-throughput in situ X-ray screening of and data collection from soluble and membrane-protein crystals at room temperature (20-25°C) and under cryogenic conditions. The Mylar in situ method uses Mylar-based film sandwich plates that are inexpensive, easy to make, and compatible with automated imaging, and that show very low background scattering. They support crystallization in microbatch and vapor-diffusion modes, as well as in lipidic cubic phases (LCPs). A set of 3D-printed holders for differently sized patches of Mylar sandwich films makes the method robust and versatile, allows for storage and shipping of crystals, and enables automated mounting at synchrotrons, as well as goniometer-based screening and data collection. The protocol covers preparation of in situ plates and setup of crystallization trials; 3D printing and assembly of holders; opening of plates, isolation of film patches containing crystals, and loading them onto holders; basic screening and data-collection guidelines; and unloading of holders, as well as reuse and recycling of them. In situ plates are prepared and assembled in 1 h; holders are 3D-printed and assembled in ≤90 min; and an in situ plate is opened, and a film patch containing crystals is isolated and loaded onto a holder in 5 min.
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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.