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Acknowledge the BioKEM Facility and Author the Staff

Why acknowledge the facility

Acknowledging the BioKEM Facility and including facility staff as authors, when appropriate, helps demonstrate the facility’s impact across ���ӽ紫ý and beyond. We track publications, presentations, and user activity to highlight the facility’s contributions to research and training for our home department, the University of Colorado Boulder, and funding agencies such as the NIH and NSF. These metrics help support requests for additional resources, which can reduce user costs and enable the acquisition of new equipment, services, and staff.

Acknowledgement and authorship guidelines

Any publication, presentation, poster, or other public display that includes data collected with support from the BioKEM Facility must acknowledge the facility and staff member as appropriate.

If BioKEM staff provided routine support, such as sample loading or standard sample screening, acknowledgement of the facility is required.

If BioKEM staff made intellectual or technical contributions, such as collecting data the user lab could not have acquired independently, assisting with data processing, advising on improvements to sample and data quality, or generating final maps or models, middle co-authorship is required. Primary or corresponding authorship is only appropriate if the project utilized staff expertise to that level of contribution for the published work.����

If you are unsure whether co-authorship is appropriate, please contact facility staff.

Acknowledgement statement

CryoEM imaging was assisted by Dr. Erik Hartwick, and data collection was performed at the Biochemistry Krios Electron Microscopy Facility (BioKEM) at ���ӽ紫ý (RRID: SCR_019057).

Authorship information

Name: Erik W. Hartwick

Affiliation: Biochemistry Krios Electron Microscopy Facility, Department of Biochemistry, University of Colorado Boulder, Boulder, CO, USA

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See Acknowledgement Section:��

Song, Jiarui, Liqi Yao, Anne R. Gooding, et al. “RNA-Induced PRC2 Inhibition Depends on the Sequence of Bound RNA.” Research Square, November 20, 2025, rs.3.rs-7963476. .

Authorship:

Tak, Uday, Kate Schinkel, Peace Walth, Jian Wei Tay, Erik W. Hartwick, and Aaron T. Whiteley. “Bacterial 2′,3′-cGAMP Activates a SAVED Effector to Form Membrane-Disrupting Filaments and Restrict Phage Replication.” Cell Host & Microbe, March 2026, S1931312826000910.

[1] U. Tak, K. Schinkel, P. Walth, J. W. Tay, E. W. Hartwick, and A. T. Whiteley, “Bacterial 2′,3′-cGAMP Activates a SAVED Effector to Form Membrane-Disrupting Filaments and Restrict Phage Replication,” Cell Host & Microbe, Mar. 2026, S1931312826000910, doi: .

[2] J. Song et al., “RNA-induced PRC2 inhibition depends on the sequence of bound RNA,” bioRxiv, p. 2024.08.29.610323, Sep. 2025, doi: .

[3] S. Shi et al., “Cryo-EM structures reveal the PP2A-B55α and Eya3 interaction that can be disrupted by a peptide inhibitor,” bioRxiv, p. 2025.02.04.636346, Feb. 2025, doi: .

[4] A. Villalta, H. Bisio, C. M. Toner, C. Abergel, and K. Luger, “Melbournevirus encodes a shorter H2B-H2A doublet histone variant that forms structurally distinct nucleosome structures,” Molecular Biology, Jan. 16, 2025, doi: .

[5] C. M. Toner, N. M. Hoitsma, S. Weerawarana, and K. Luger, “Characterization of Medusavirus encoded histones reveals nucleosome-like structures and a unique linker histone,” Nat Commun, vol. 15, no. 1, p. 9138, Oct. 2024, doi: .

[6] J. Song et al., “Structural basis for inactivation of PRC2 by G-quadruplex RNA,” Science, vol. 381, no. 6664, pp. 1331–1337, Sep. 2023, doi: .

[7] L. I. Jansson-Fritzberg et al., “DNMT1 inhibition by pUG-fold quadruplex RNA,” RNA, vol. 29, no. 3, pp. 346–360, Mar. 2023, doi: .

[8] J. A. Bennett, L. R. Steward, J. Rudolph, A. P. Voss, and H. Aydin, “The structure of the human LACTB filament reveals the mechanisms of assembly and membrane binding,” PLoS Biol, vol. 20, no. 12, p. e3001899, Dec. 2022, doi: .

[9] E. Zamponi, J. B. Meehl, and G. K. Voeltz, “The ER ladder is a unique morphological feature of developing mammalian axons,” Dev Cell, vol. 57, no. 11, pp. 1369–1382.e6, Jun. 2022, doi: .

[10] K. Zhou et al., “CENP-N promotes the compaction of centromeric chromatin,” Nat Struct Mol Biol, vol. 29, no. 4, pp. 403–413, Apr. 2022, doi: .