Evidence map›Paper›PMID 30082514›Full record

ArticleActa crystallographica. Section D, Structural biology2018

Cryoprotectant-free high-pressure cooling and dynamic nuclear polarization for more sensitive detection of hydrogen in neutron protein crystallography.

Ichiro Tanaka, Naoya Komatsuzaki, Wen Xue Yue, Toshiyuki Chatake, Katsuhiro Kusaka, Nobuo Niimura, Daisuke Miura, Takahiro Iwata, Yoshiyuki Miyachi, Genki Nukazuka and 1 more

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Article in Acta crystallographica. Section D, Structural biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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4 · The record

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5 · Who and what money

Authors and funding

11 authors.

Ichiro TanakaCollege of Engineering, Ibaraki University, Hitachi, Ibaraki 316-8511, Japan.
Naoya KomatsuzakiGraduate School of Science and Engineering, Ibaraki University, Hitachi, Ibaraki 316-8511, Japan.
Wen Xue YueGraduate School of Science and Engineering, Ibaraki University, Hitachi, Ibaraki 316-8511, Japan.
Toshiyuki ChatakeResearch Reactor Institute, Kyoto University, Kumatori, Osaka 590-0494, Japan.
Katsuhiro KusakaFrontier Research Center for Applied Atomic Sciences, Ibaraki University, Tokai, Ibaraki 319-1106, Japan.
Nobuo NiimuraFrontier Research Center for Applied Atomic Sciences, Ibaraki University, Tokai, Ibaraki 319-1106, Japan.
Daisuke MiuraFaculty of Science, Yamagata University, Yamagata, Yamagata 990-8560, Japan.
Takahiro IwataFaculty of Science, Yamagata University, Yamagata, Yamagata 990-8560, Japan.
Yoshiyuki MiyachiFaculty of Science, Yamagata University, Yamagata, Yamagata 990-8560, Japan.
Genki NukazukaFaculty of Science, Yamagata University, Yamagata, Yamagata 990-8560, Japan.
Hiroki MatsudaFaculty of Science, Yamagata University, Yamagata, Yamagata 990-8560, Japan.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

To improve the sensitivity of hydrogen detection using neutrons, a proton-polarization technique together with a high-pressure cooling method is necessary. The highest pressure (200 MPa) used in the experiment described here enabled relatively large protein crystals to be cooled without any cryoprotectants while retaining the protein structure, and it was confirmed that high-pressure-cooled crystals diffracted to nearly the same resolution as flash-cooled small crystals soaked with cryoprotectants. Dynamic nuclear polarization was used as a proton-polarization technique for protein crystals, and ∼300 mg polycrystalline protein doped with TEMPOL gave a maximum proton polarization of 22.3% at a temperature of 0.5 K in a 2.5 T magnetic field.

Indexed as

Cold TemperatureCrystallographyCyclic N-OxidesElectron Spin Resonance SpectroscopyHydrogenMuramidaseNeutron DiffractionPressureProteinsSpin LabelsCyclic N-OxidesHydrogenMuramidaseProteinsSpin Labelstempoldynamic nuclear polarizationhigh-pressure coolinghydrogen sensitivityneutron protein crystallography

Identifiers

PMID30082514
PMCPMC6079630

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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.