ReviewArchives of biochemistry and biophysics2016
Assessment of microcrystal quality by transmission electron microscopy for efficient serial femtosecond crystallography.
Review in Archives of biochemistry and biophysics, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 20 citations in OpenAlex.
- Review
- Comprehensive microcrystal electron diffraction sample preparation for cryo-EM.Nature protocols · 2025Review
- High-Throughput Identification of Crystalline Natural Products from Crude Extracts Enabled by Microarray Technology and microED.ACS central science · 2024Article
- MicroED Sample Preparation and Data Collection For Protein Crystals.Methods in molecular biology (Clifton, N.J.) · 2021Article
- Detection of Microcrystals for CryoEM.Methods in molecular biology (Clifton, N.J.) · 2021Article
- The cryo-EM method microcrystal electron diffraction (MicroED).Nature methods · 2019Review
- Transcription with a laser: Radiation-damage-free diffraction of RNA Polymerase II crystals.Methods (San Diego, Calif.) · 2019Article
- Strategies for sample delivery for femtosecond crystallography.Acta crystallographica. Section D, Structural biology · 2019Review
- MicroED: a versatile cryoEM method for structure determination.Emerging topics in life sciences · 2018Article
- A new apatinib microcrystal formulation enhances the effect of radiofrequency ablation treatment on hepatocellular carcinoma.OncoTargets and therapy · 2018Article
- MicroED Structure of AuThe journal of physical chemistry letters · 2017Article
- A Bright Future for Serial Femtosecond Crystallography with XFELs.Trends in biochemical sciences · 2017Review
Corrections and comments
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Authors and funding
9 authors at 4 institutions in 1 country.
Funding
Abstract
Serial femtosecond crystallography (SFX) employing high-intensity X-ray free-electron laser (XFEL) sources has enabled structural studies on microcrystalline protein samples at non-cryogenic temperatures. However, the identification and optimization of conditions that produce well diffracting microcrystals remains an experimental challenge. Here, we report parallel SFX and transmission electron microscopy (TEM) experiments using fragmented microcrystals of wild type (WT) homoprotocatechuate 2,3-dioxygenase (HPCD) and an active site variant (H200Q). Despite identical crystallization conditions and morphology, as well as similar crystal size and density, the indexing efficiency of the diffraction data collected using the H200Q variant sample was over 7-fold higher compared to the diffraction results obtained using the WT sample. TEM analysis revealed an abundance of protein aggregates, crystal conglomerates and a smaller population of highly ordered lattices in the WT sample as compared to the H200Q variant sample. While not reported herein, the 1.75 Å resolution structure of the H200Q variant was determined from ∼16 min of beam time, demonstrating the utility of TEM analysis in evaluating sample monodispersity and lattice quality, parameters critical to the efficiency of SFX experiments.
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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.