ArticleActa crystallographica. Section F, Structural biology and crystallization communications2008
A preliminary neutron crystallographic study of thaumatin.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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.
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.
Who cites it
6 citing papers in PubMed.
- Preliminary neutron crystallographic study of human transthyretin.Acta crystallographica. Section F, Structural biology and crystallization communications · 2011Article
- High-resolution structure of the recombinant sweet-tasting protein thaumatin I.Acta crystallographica. Section F, Structural biology and crystallization communications · 2011Article
- Neutron fibre diffraction studies of amyloid using H2O/D2O isotopic replacement.Acta crystallographica. Section F, Structural biology and crystallization communications · 2011Article
- A preliminary neutron crystallographic study of an A-DNA crystal.Acta crystallographica. Section F, Structural biology and crystallization communications · 2009Article
- A preliminary neutron diffraction study of gamma-chymotrypsin.Acta crystallographica. Section F, Structural biology and crystallization communications · 2009Article
- Neutron crystallography: opportunities, challenges, and limitations.Current opinion in structural biology · 2008Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A preliminary neutron crystallographic study of the sweet protein thaumatin is presented. Large hydrogenated crystals were prepared in deuterated crystallization buffer using the gel-acupuncture method. Data were collected to a resolution of 2 A on the LADI-III diffractometer at the Institut Laue Langevin (ILL). The results demonstrate the feasibility of a full neutron crystallographic analysis of this structure aimed at providing relevant information on the location of H atoms, the distribution of charge on the protein surface and localized water in the structure. This information will be of interest for understanding the specificity of thaumatin-receptor interactions and will contribute to further understanding of the molecular mechanisms underlying the perception of taste.
Indexed as
Identifiers
What OpenQuestion holds
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.