Cargando…

The oxygen-oxygen distance of water in crystallographic data sets

Water is a key component of cellular biochemistry and numerous water molecules are visible in crystallographic structures. Here we report a series of data sets of crystallographic water: a high resolution data set, a cytochrome c oxidase (subunit I) data set and a carbonic anhydrase data set. These...

Descripción completa

Detalles Bibliográficos
Autor principal: Palese, Luigi Leonardo
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6965711/
https://www.ncbi.nlm.nih.gov/pubmed/31970272
http://dx.doi.org/10.1016/j.dib.2019.105076
_version_ 1783488666232946688
author Palese, Luigi Leonardo
author_facet Palese, Luigi Leonardo
author_sort Palese, Luigi Leonardo
collection PubMed
description Water is a key component of cellular biochemistry and numerous water molecules are visible in crystallographic structures. Here we report a series of data sets of crystallographic water: a high resolution data set, a cytochrome c oxidase (subunit I) data set and a carbonic anhydrase data set. These data support the evidence that short distance water molecule pairs are present both at the surface and inside the cavities of proteins. These data are related to article entitled “Oxygen-oxygen distances in protein-bound crystallographic water suggest the presence of protonated clusters” (Palese, 2020) [1].
format Online
Article
Text
id pubmed-6965711
institution National Center for Biotechnology Information
language English
publishDate 2020
publisher Elsevier
record_format MEDLINE/PubMed
spelling pubmed-69657112020-01-22 The oxygen-oxygen distance of water in crystallographic data sets Palese, Luigi Leonardo Data Brief Biochemistry, Genetics and Molecular Biology Water is a key component of cellular biochemistry and numerous water molecules are visible in crystallographic structures. Here we report a series of data sets of crystallographic water: a high resolution data set, a cytochrome c oxidase (subunit I) data set and a carbonic anhydrase data set. These data support the evidence that short distance water molecule pairs are present both at the surface and inside the cavities of proteins. These data are related to article entitled “Oxygen-oxygen distances in protein-bound crystallographic water suggest the presence of protonated clusters” (Palese, 2020) [1]. Elsevier 2020-01-07 /pmc/articles/PMC6965711/ /pubmed/31970272 http://dx.doi.org/10.1016/j.dib.2019.105076 Text en © 2020 The Author http://creativecommons.org/licenses/by-nc-nd/4.0/ This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).
spellingShingle Biochemistry, Genetics and Molecular Biology
Palese, Luigi Leonardo
The oxygen-oxygen distance of water in crystallographic data sets
title The oxygen-oxygen distance of water in crystallographic data sets
title_full The oxygen-oxygen distance of water in crystallographic data sets
title_fullStr The oxygen-oxygen distance of water in crystallographic data sets
title_full_unstemmed The oxygen-oxygen distance of water in crystallographic data sets
title_short The oxygen-oxygen distance of water in crystallographic data sets
title_sort oxygen-oxygen distance of water in crystallographic data sets
topic Biochemistry, Genetics and Molecular Biology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6965711/
https://www.ncbi.nlm.nih.gov/pubmed/31970272
http://dx.doi.org/10.1016/j.dib.2019.105076
work_keys_str_mv AT paleseluigileonardo theoxygenoxygendistanceofwaterincrystallographicdatasets
AT paleseluigileonardo oxygenoxygendistanceofwaterincrystallographicdatasets