Re-evaluation of protein neutron crystallography with and without X-ray/neutron joint refinement.

X-ray/neutron joint refinement copper amine oxidases neutron crystallography quinone cofactor

Journal

IUCrJ
ISSN: 2052-2525
Titre abrégé: IUCrJ
Pays: England
ID NLM: 101623101

Informations de publication

Date de publication:
01 May 2022
Historique:
received: 02 02 2022
accepted: 01 04 2022
entrez: 13 5 2022
pubmed: 14 5 2022
medline: 14 5 2022
Statut: epublish

Résumé

Protein neutron crystallography is a powerful technique to determine the positions of H atoms, providing crucial biochemical information such as the protonation states of catalytic groups and the geometry of hydrogen bonds. Recently, the crystal structure of a bacterial copper amine oxidase was determined by joint refinement using X-ray and neutron diffraction data sets at resolutions of 1.14 and 1.72 Å, respectively [Murakawa

Identifiants

pubmed: 35546796
doi: 10.1107/S2052252522003657
pii: S2052252522003657
pmc: PMC9067118
doi:

Types de publication

Journal Article

Langues

eng

Pagination

342-348

Informations de copyright

© Takeshi Murakawa et al. 2022.

Références

FEBS Lett. 1994 Sep 12;351(3):360-4
pubmed: 8082796
Nature. 2016 May 18;534(7606):281-4
pubmed: 27279229
J Vis Exp. 2020 Dec 1;(166):
pubmed: 33346193
Annu Rev Biochem. 1994;63:299-344
pubmed: 7979241
J Am Chem Soc. 2015 Apr 29;137(16):5452-60
pubmed: 25872660
Nat Struct Biol. 2002 Aug;9(8):591-6
pubmed: 12134140
Methods Enzymol. 2020;634:177-199
pubmed: 32093832
Proc Natl Acad Sci U S A. 2009 Jan 13;106(2):440-4
pubmed: 19122140
Acta Crystallogr D Struct Biol. 2017 Feb 1;73(Pt 2):148-157
pubmed: 28177311
Biochemistry. 2006 Apr 4;45(13):4105-20
pubmed: 16566584
Proc Natl Acad Sci U S A. 2020 May 19;117(20):10818-10824
pubmed: 32371483
Methods Enzymol. 2020;634:101-123
pubmed: 32093829
Acta Crystallogr D Biol Crystallogr. 2010 Jan;66(Pt 1):12-21
pubmed: 20057044
Acta Crystallogr D Biol Crystallogr. 1998 Sep 1;54(Pt 5):905-21
pubmed: 9757107
Acta Crystallogr D Biol Crystallogr. 2010 Nov;66(Pt 11):1153-63
pubmed: 21041930
Proc Natl Acad Sci U S A. 2008 Feb 12;105(6):1844-8
pubmed: 18250329
Acta Crystallogr D Biol Crystallogr. 2010 Apr;66(Pt 4):486-501
pubmed: 20383002
Int J Mol Sci. 2012;13(5):5375-405
pubmed: 22754303
RSC Adv. 2020 Oct 21;10(63):38631-38639
pubmed: 35517562
J Am Chem Soc. 2003 Jan 29;125(4):1041-55
pubmed: 12537504
Acta Crystallogr D Struct Biol. 2019 Oct 1;75(Pt 10):861-877
pubmed: 31588918
Acta Crystallogr D Biol Crystallogr. 2010 Feb;66(Pt 2):125-32
pubmed: 20124692
Acta Crystallogr D Biol Crystallogr. 2009 Jun;65(Pt 6):567-73
pubmed: 19465771
J Appl Crystallogr. 2007 Aug 1;40(Pt 4):658-674
pubmed: 19461840
Acta Crystallogr D Biol Crystallogr. 2013 Dec;69(Pt 12):2483-94
pubmed: 24311589
Nature. 2015 Apr 23;520(7548):571-4
pubmed: 25624102
Acta Crystallogr D Struct Biol. 2018 Nov 1;74(Pt 11):1041-1052
pubmed: 30387763
J Synchrotron Radiat. 2013 Nov;20(Pt 6):994-8
pubmed: 24121355

Auteurs

Takeshi Murakawa (T)

Department of Biochemistry, Faculty of Medicine, Osaka Medical and Pharmaceutical University, 2-7 Daigakumachi, Takatsuki, Osaka 569-8686, Japan.

Kazuo Kurihara (K)

Institute for Quantum Life Science, Quantum Life and Medical Science Directorate, National Institutes for Quantum Science and Technology, 2-4 Shirakata, Tokai, Ibaraki 319-1106, Japan.

Motoyasu Adachi (M)

Institute for Quantum Life Science, Quantum Life and Medical Science Directorate, National Institutes for Quantum Science and Technology, 2-4 Shirakata, Tokai, Ibaraki 319-1106, Japan.

Katsuhiro Kusaka (K)

Frontier Research Center for Applied Atomic Sciences, Ibaraki University, 162-1 Shirakata, Tokai, Ibaraki 319-1106, Japan.

Katsuyuki Tanizawa (K)

Institute of Scientific and Industrial Research (SANKEN), Osaka University, 8-1 Mihogaoka, Ibaraki, Osaka 567-0047, Japan.

Toshihide Okajima (T)

Institute of Scientific and Industrial Research (SANKEN), Osaka University, 8-1 Mihogaoka, Ibaraki, Osaka 567-0047, Japan.

Classifications MeSH