Evidence map›Paper›PMID 32915778›Full record

ArticlePloS one2020

Rapid and robust antibody Fab fragment crystallization utilizing edge-to-edge beta-sheet packing.

Ricky Lieu, Stephen Antonysamy, Zhanna Druzina, Carolyn Ho, N Rebecca Kang, Anna Pustilnik, Jing Wang, Shane Atwell

Erratum issuedAbstract read
In one paragraph

Article in PloS one, 2020. 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 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing 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.

3 · Its place in the literature

Who cites it

29 citing papers in PubMed.

  1. Article
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  3. Structural basis of membrane engagement and polyreactivity control in HIV-1 MPER broadly neutralizing antibodies.Proceedings of the National Academy of Sciences of the United States of America · 2026
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  10. Human coronavirus HKU1 neutralization by glycan receptor mimicry.bioRxiv : the preprint server for biology · 2025
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors.

Ricky LieuBiotechnology Discovery Research, Applied Molecular Evolution, Eli Lilly and Company, San Diego, CA, United States of America.
Stephen AntonysamyDiscovery Chemistry Research and Technologies, Eli Lilly and Company Corporate Center, Indianapolis, IN, United States of America.
Zhanna DruzinaDiscovery Chemistry Research and Technologies, Eli Lilly and Company Corporate Center, Indianapolis, IN, United States of America.
Carolyn HoBiotechnology Discovery Research, Applied Molecular Evolution, Eli Lilly and Company, San Diego, CA, United States of America.
N Rebecca KangBiotechnology Discovery Research, Applied Molecular Evolution, Eli Lilly and Company, San Diego, CA, United States of America.
Anna PustilnikDiscovery Chemistry Research and Technologies, Eli Lilly and Company Corporate Center, Indianapolis, IN, United States of America.
Jing WangDiscovery Chemistry Research and Technologies, Eli Lilly and Company Corporate Center, Indianapolis, IN, United States of America.
Shane AtwellBiotechnology Discovery Research, Applied Molecular Evolution, Eli Lilly and Company, San Diego, CA, United States of America.ORCID 0000-0002-2578-2462

Funding

User Training and OutreachP30GM124169 · NIGMS · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI PAUL David ADAMS, Gregory L Hura · 2017 to 2026
$28.6M
NIGMS NIH HHS P30 GM124169
6 · The paper itself

Abstract

Antibody therapeutics are one of the most important classes of drugs. Antibody structures have become an integral part of predicting the behavior of potential therapeutics, either directly or as the basis of modeling. Structures of Fab:antigen complexes have even greater value. While the crystallization and structure determination of Fabs is easy relative to many other protein classes, especially membrane proteins, broad screening and optimization of crystalline hits is still necessary. Through a comprehensive review of rabbit Fab crystal contacts and their incompatibility with human Fabs, we identified a small secondary structural element from the rabbit light chain constant domain potentially responsible for hindering the crystallization of human Fabs. Upon replacing the human kappa constant domain FG loop (HQGLSSP) with the two residue shorter rabbit loop (QGTTS), we dramatically improved the crystallization of human Fabs and Fab:antigen complexes. Our design, which we call "Crystal Kappa", enables rapid crystallization of human fabs and fab complexes in a broad range of conditions, with less material in smaller screens or from dilute solutions.

Indexed as

Amino Acid SequenceAnimalsCHO CellsCricetulusCrystallizationCrystallography, X-RayHumansImmunoglobulin Fab FragmentsImmunoglobulin kappa-ChainsProtein Conformation, beta-StrandRabbitsImmunoglobulin Fab FragmentsImmunoglobulin kappa-Chains

Identifiers

PMID32915778
PMCPMC7485759

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

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.