Evidence map›Paper›PMID 39222305›Full record

ArticleActa crystallographica. Section D, Structural biology2024

Comparison of two crystal polymorphs of NowGFP reveals a new conformational state trapped by crystal packing.

Jin Kyun Kim, Hannah Jeong, Jeongwoo Seo, Seoyoon Kim, Kyung Hyun Kim, Duyoung Min, Chae Un Kim

Abstract readComparative Study
PubMed Full text at PMC Publisher
In one paragraph

Article in Acta crystallographica. Section D, Structural biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. 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.

3 · Its place in the literature

Who cites it

1 citing paper in PubMed.

  1. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors.

Jin Kyun KimDepartment of Physics, Ulsan National Institute of Science and Technology (UNIST), Ulsan 44919, Republic of Korea.ORCID 0000-0003-2650-9879
Hannah JeongDepartment of Physics, Ulsan National Institute of Science and Technology (UNIST), Ulsan 44919, Republic of Korea.ORCID 0009-0004-4494-2283
Jeongwoo SeoDepartment of Physics, Ulsan National Institute of Science and Technology (UNIST), Ulsan 44919, Republic of Korea.
Seoyoon KimDepartment of Chemistry, Ulsan National Institute of Science and Technology (UNIST), Ulsan 44919, Republic of Korea.
Kyung Hyun KimDepartment of Biotechnology and Bioinformatics, Korea University, Sejong 30019, Republic of Korea.
Duyoung MinDepartment of Chemistry, Ulsan National Institute of Science and Technology (UNIST), Ulsan 44919, Republic of Korea.
Chae Un KimDepartment of Physics, Ulsan National Institute of Science and Technology (UNIST), Ulsan 44919, Republic of Korea.ORCID 0000-0001-9350-8441

Funding

National Research Foundation of Korea NRF-2020R1C1C1003937National Research Foundation of Korea NRF-2022R1A2C2091815
6 · The paper itself

Abstract

Crystal polymorphism serves as a strategy to study the conformational flexibility of proteins. However, the relationship between protein crystal packing and protein conformation often remains elusive. In this study, two distinct crystal forms of a green fluorescent protein variant, NowGFP, are compared: a previously identified monoclinic form (space group C2) and a newly discovered orthorhombic form (space group P2

Indexed as

Green Fluorescent ProteinsModels, MolecularProtein ConformationCrystallizationCrystallography, X-RayGreen Fluorescent Proteinsconformational flexibilitycrystal polymorphismfluorescent proteinsNowGFPprotein crystallizationprotein crystal packing

Identifiers

PMID39222305
PMCPMC11394120

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Registered trials

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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.