Microcrystal preparation for serial femtosecond X-ray crystallography of bacterial copper amine oxidase.


Journal

Acta crystallographica. Section F, Structural biology communications
ISSN: 2053-230X
Titre abrégé: Acta Crystallogr F Struct Biol Commun
Pays: United States
ID NLM: 101620319

Informations de publication

Date de publication:
01 Oct 2021
Historique:
received: 09 07 2021
accepted: 28 08 2021
entrez: 4 10 2021
pubmed: 5 10 2021
medline: 1 2 2022
Statut: ppublish

Résumé

Recent advances in serial femtosecond X-ray crystallography (SFX) using X-ray free-electron lasers have paved the way for determining radiation-damage-free protein structures under nonfreezing conditions. However, the large-scale preparation of high-quality microcrystals of uniform size is a prerequisite for SFX, and this has been a barrier to its widespread application. Here, a convenient method for preparing high-quality microcrystals of a bacterial quinoprotein enzyme, copper amine oxidase from Arthrobacter globiformis, is reported. The method consists of the mechanical crushing of large crystals (5-15 mm

Identifiants

pubmed: 34605440
pii: S2053230X21008967
doi: 10.1107/S2053230X21008967
pmc: PMC8488853
doi:

Substances chimiques

Amine Oxidase (Copper-Containing) EC 1.4.3.21

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

356-363

Subventions

Organisme : Japan Society for the Promotion of Science
ID : 20H05448
Organisme : Japan Society for the Promotion of Science
ID : 19H05781
Organisme : Japan Society for the Promotion of Science
ID : 19K05694
Organisme : Japan Agency for Medical Research and Development
ID : JP20am0101070
Organisme : Japan Agency for Medical Research and Development
ID : JP21am0101070 (support number 2302)

Références

J Synchrotron Radiat. 2015 May;22(3):571-6
pubmed: 25931070
IUCrJ. 2019 Jun 23;6(Pt 4):761-772
pubmed: 31316819
Acta Crystallogr A Found Adv. 2019 Sep 1;75(Pt 5):694-704
pubmed: 31475914
Acta Crystallogr D Biol Crystallogr. 2012 May;68(Pt 5):564-77
pubmed: 22525754
J Appl Crystallogr. 2016 Mar 29;49(Pt 2):680-689
pubmed: 27047311
Nat Struct Biol. 2002 Aug;9(8):591-6
pubmed: 12134140
Acta Crystallogr D Biol Crystallogr. 2010 Apr;66(Pt 4):486-501
pubmed: 20383002
Acta Crystallogr F Struct Biol Commun. 2018 Jun 1;74(Pt 6):327-330
pubmed: 29870015
J Am Chem Soc. 2003 Jan 29;125(4):1041-55
pubmed: 12537504
J Synchrotron Radiat. 2015 May;22(3):532-7
pubmed: 25931065
Nat Methods. 2014 Jul;11(7):734-6
pubmed: 24813624
Nature. 2000 Aug 17;406(6797):752-7
pubmed: 10963603
J Appl Crystallogr. 2014 May 29;47(Pt 3):1118-1131
pubmed: 24904246
Sci Rep. 2017 Apr 6;7(1):703
pubmed: 28386083
Nat Methods. 2015 Jan;12(1):61-3
pubmed: 25384243
Science. 2014 Dec 5;346(6214):1242-6
pubmed: 25477465
J Appl Crystallogr. 2016 Apr 18;49(Pt 3):1035-1041
pubmed: 27275146
Acta Crystallogr D Biol Crystallogr. 2015 Dec 1;71(Pt 12):2519-25
pubmed: 26627659
FEBS Lett. 1994 Sep 12;351(3):360-4
pubmed: 8082796
Biochemistry. 2006 Apr 4;45(13):4105-20
pubmed: 16566584
IUCrJ. 2018 Jan 01;5(Pt 1):22-31
pubmed: 29354268
J Appl Crystallogr. 2019 Oct 17;52(Pt 6):1280-1288
pubmed: 31798359
Science. 2016 Dec 23;354(6319):1552-1557
pubmed: 28008064
Proc Natl Acad Sci U S A. 2020 May 19;117(20):10818-10824
pubmed: 32371483
Opt Express. 2015 Nov 2;23(22):28459-70
pubmed: 26561117
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
Science. 2015 Oct 23;350(6259):445-50
pubmed: 26359336
Nature. 2017 Jan 12;541(7636):242-246
pubmed: 27841871
Rev Sci Instrum. 2014 Mar;85(3):033110
pubmed: 24689567

Auteurs

Takeshi Murakawa (T)

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

Mamoru Suzuki (M)

Institute for Protein Research, Osaka University, 3-2 Yamadaoka, Suita, Osaka 565-0871, Japan.

Toshi Arima (T)

SPring-8 Center, RIKEN, 1-1-1 Kouto, Sayo-cho, Sayo-gun, Hyogo 679-5148, Japan.

Michihiro Sugahara (M)

SPring-8 Center, RIKEN, 1-1-1 Kouto, Sayo-cho, Sayo-gun, Hyogo 679-5148, Japan.

Tomoyuki Tanaka (T)

SPring-8 Center, RIKEN, 1-1-1 Kouto, Sayo-cho, Sayo-gun, Hyogo 679-5148, Japan.

Rie Tanaka (R)

SPring-8 Center, RIKEN, 1-1-1 Kouto, Sayo-cho, Sayo-gun, Hyogo 679-5148, Japan.

So Iwata (S)

SPring-8 Center, RIKEN, 1-1-1 Kouto, Sayo-cho, Sayo-gun, Hyogo 679-5148, Japan.

Eriko Nango (E)

SPring-8 Center, RIKEN, 1-1-1 Kouto, Sayo-cho, Sayo-gun, Hyogo 679-5148, Japan.

Kensuke Tono (K)

SPring-8 Center, RIKEN, 1-1-1 Kouto, Sayo-cho, Sayo-gun, Hyogo 679-5148, Japan.

Hideyuki Hayashi (H)

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

Kenji Fukui (K)

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

Takato Yano (T)

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

Katsuyuki Tanizawa (K)

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

Toshihide Okajima (T)

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

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