Lysozyme revisited
(2025) In Structure 33(1). p.6-7- Abstract
Lysozyme is a model system for crystallographers. In this issue of Structure, Ramos et al. report atomic resolution neutron structures of lysozyme, which unambiguously show the protonation states and hydrogen-bonding networks of the active site. This resolves mechanistic questions that have been debated for decades and provides a unique view to a protein at atomic detail.
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/516fd517-a61d-470d-a089-def387e00acf
- author
- Oksanen, Esko LU
- organization
- publishing date
- 2025-01
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Structure
- volume
- 33
- issue
- 1
- pages
- 2 pages
- publisher
- Cell Press
- external identifiers
-
- pmid:39753102
- scopus:85213033276
- ISSN
- 0969-2126
- DOI
- 10.1016/j.str.2024.12.005
- language
- English
- LU publication?
- yes
- id
- 516fd517-a61d-470d-a089-def387e00acf
- date added to LUP
- 2025-03-04 10:37:39
- date last changed
- 2025-07-08 21:39:28
@misc{516fd517-a61d-470d-a089-def387e00acf,
abstract = {{<p>Lysozyme is a model system for crystallographers. In this issue of Structure, Ramos et al. report atomic resolution neutron structures of lysozyme, which unambiguously show the protonation states and hydrogen-bonding networks of the active site. This resolves mechanistic questions that have been debated for decades and provides a unique view to a protein at atomic detail.</p>}},
author = {{Oksanen, Esko}},
issn = {{0969-2126}},
language = {{eng}},
number = {{1}},
pages = {{6--7}},
publisher = {{Cell Press}},
series = {{Structure}},
title = {{Lysozyme revisited}},
url = {{http://dx.doi.org/10.1016/j.str.2024.12.005}},
doi = {{10.1016/j.str.2024.12.005}},
volume = {{33}},
year = {{2025}},
}