Article in Acta crystallographica. Section D, Structural biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 1 paper.
0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
2 · The registry
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Maria J Pedroza RomoDepartment of Chemistry and Biochemistry, Brigham Young University, 701 East University Parkway, Provo, UT 84602, USA.ORCID 0000-0002-7441-3874
Alihikaua KeliilikiDepartment of Chemistry and Biochemistry, Brigham Young University, 701 East University Parkway, Provo, UT 84602, USA.
Jacob C AverettDepartment of Chemistry and Biochemistry, Brigham Young University, 701 East University Parkway, Provo, UT 84602, USA.ORCID 0000-0002-2287-1590
Joseph F GonzalezDepartment of Chemistry and Biochemistry, Brigham Young University, 701 East University Parkway, Provo, UT 84602, USA.
Ethan NoakesDepartment of Chemistry and Biochemistry, Brigham Young University, 701 East University Parkway, Provo, UT 84602, USA.ORCID 0009-0007-6957-3295
Elijah W WilsonDepartment of Chemistry and Biochemistry, Brigham Young University, 701 East University Parkway, Provo, UT 84602, USA.ORCID 0000-0001-5009-2685
Conrad SmithDepartment of Chemistry and Biochemistry, Brigham Young University, 701 East University Parkway, Provo, UT 84602, USA.ORCID 0009-0007-0142-893X
Blake AverettDepartment of Chemistry and Biochemistry, Brigham Young University, 701 East University Parkway, Provo, UT 84602, USA.ORCID 0009-0001-0255-9516
Dalton HansenDepartment of Chemistry and Biochemistry, Brigham Young University, 701 East University Parkway, Provo, UT 84602, USA.ORCID 0009-0009-5764-5524
Riley NicklesDepartment of Chemistry and Biochemistry, Brigham Young University, 701 East University Parkway, Provo, UT 84602, USA.ORCID 0009-0009-5570-9096
Miles BradfordDepartment of Chemistry and Biochemistry, Brigham Young University, 701 East University Parkway, Provo, UT 84602, USA.ORCID 0009-0004-8380-4975
Sara SoleimaniDepartment of Chemistry and Biochemistry, Brigham Young University, 701 East University Parkway, Provo, UT 84602, USA.ORCID 0000-0001-8676-8966
Tobin SmithDepartment of Chemistry and Biochemistry, Brigham Young University, 701 East University Parkway, Provo, UT 84602, USA.
Supeshala NawarathnageDepartment of Chemistry and Biochemistry, Brigham Young University, 701 East University Parkway, Provo, UT 84602, USA.ORCID 0000-0002-8850-6625
Prasadika SamarwickramaDepartment of Chemistry and Biochemistry, Brigham Young University, 701 East University Parkway, Provo, UT 84602, USA.
Ariel KelschDepartment of Chemistry and Biochemistry, Brigham Young University, 701 East University Parkway, Provo, UT 84602, USA.
Derick BunnDepartment of Chemistry and Biochemistry, Brigham Young University, 701 East University Parkway, Provo, UT 84602, USA.ORCID 0000-0002-0005-5023
Cameron StewartDepartment of Chemistry and Biochemistry, Brigham Young University, 701 East University Parkway, Provo, UT 84602, USA.
Wisdom AbiodunDepartment of Chemistry and Biochemistry, Brigham Young University, 701 East University Parkway, Provo, UT 84602, USA.
Evan TsubakiDepartment of Chemistry and Biochemistry, Brigham Young University, 701 East University Parkway, Provo, UT 84602, USA.ORCID 0009-0001-8014-9643
Seth BrownDepartment of Chemistry and Biochemistry, Brigham Young University, 701 East University Parkway, Provo, UT 84602, USA.ORCID 0000-0003-2888-7208
Tzanko I DoukovMacromolecular Crystallography Group, Structural Molecular Biology Resource, Stanford Synchrotron Radiation Lightsource, Menlo Park, CA 94025, USA.ORCID 0000-0001-8625-2572
James D MoodyDepartment of Chemistry and Biochemistry, Brigham Young University, 701 East University Parkway, Provo, UT 84602, USA.ORCID 0000-0003-2266-5348
Funding
X-ray Absorption Spectroscopy (XAS) pp.711-759P41GM103393 · NIGMS · STANFORD UNIVERSITY · PI HODGSON, KEITH O · 2012 to 2019
$30.6M
Expanding the capabilities and usage of the TELSAM protein crystallization chaperoneR35GM155011 · NIGMS · BRIGHAM YOUNG UNIVERSITY · PI James Daniel Moody · 2024 to 2026
$1.0M
TELSAM polymers are powerful crystallization chaperones meriting continued investigation (Diversity Supplement)R15GM146209 · NIGMS · BRIGHAM YOUNG UNIVERSITY · PI MOODY, JAMES DANIEL · 2022 to 2024
$520k
National Institutes of Health, National Institute of General Medical Sciences 1R35GM155011National Institutes of Health, National Institute of General Medical Sciences 3R15GM146209-01S1NIGMS NIH HHS P41 GM103393NIGMS NIH HHS R15 GM146209NIGMS NIH HHS R35 GM155011
6 · The paper itself
Abstract
Fusing a variant of the sterile alpha motif domain of the human translocation ETS leukaemia protein (1TEL) to a protein of interest has been shown to significantly enhance its crystallization propensity. 1TEL is a pH-dependent, polymer-forming protein crystallization chaperone which, when covalently fused to a protein of interest, forms a stable, well ordered crystal lattice. However, despite its success, a challenge persists in that crystal quality and diffraction limits appear to be heavily dependent on the choice of linker between 1TEL and the protein of interest, with the identification of a functional linker currently relying on trial-and-error methods. Likewise, previous studies revealed that a ten-histidine tag at the 1TEL N-terminus can either facilitate or hinder the ordered crystallization of target proteins attached via flexible or semi-flexible linkers. To address these challenges, we designed multiple constructs with several types of linkers [rigid (helical fusion), semi-flexible (Pro-Ala and Pro-Ala-Ala) and flexible (Gly-Gly and Gly-Gly-Gly)] of varying lengths to fuse either a designed ankyrin-repeat protein (DARPin) or the thirty-eight-negative kinase-1 ubiquitin-associated (UBA) domain to the 1TEL C-terminus. Semi-flexible and flexible linker constructs were made with and without a ten-histidine tag. Our findings indicate that short semi-flexible and rigid linkers consistently yielded large crystals with a DARPin target protein, but that flexible linkers performed best with a UBA-domain target protein. Removing the ten-histidine tag uniformly enhanced crystallization rates, improved the crystal morphology and increased the crystallization propensity of the semi-flexible and flexible linker constructs. These results suggest that the ideal linker selection primarily depends on the properties of the target protein. Our data support our current recommendation to use a short flexible or semi-flexible linker between 1TEL and the target protein to facilitate protein crystallization and high-resolution structure determination.
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.
Optimal 1TEL-target protein linker character is target protein-dependent. · full record | OpenQuestion