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Crystallization and preliminary X-ray diffraction study of the catalytic subunit of archaeal H+ -transporting ATP synthase from Pyrococcus horikoshii OT3.
Acta Crystallogr D Biol Crystallogr. 2004 Aug; 60(Pt 8):1484-6.AC

Abstract

H+ -transporting ATP synthase (H+ -ATPase) is a multi-subunit complex which acts to produce ATP molecules. The catalytic subunit A of the archaeal-type H+ -ATPase from Pyrococcus horikoshii OT3 was cloned, expressed in Escherichia coli, purified and crystallized by the hanging-drop vapour-diffusion method with MPD as a precipitant. X-ray intensity data were collected to 2.55 A resolution at beamline BL41XU of SPring-8. The crystals belong to the tetragonal space group P4(1)2(1)2 or P4(3)2(1)2, with unit-cell parameters a = b = 128.0, c = 104.7 A, and contain one molecule per asymmetric unit.

Authors+Show Affiliations

Maegawa Y
Division of Biological Sciences, Graduate School of Science, Hokkaido University, Sapporo 060-0810, Japan.
Morita H
No affiliation info available
Yao M
No affiliation info available
Watanabe N
No affiliation info available
Tanaka I
No affiliation info available

MeSH

Catalytic DomainCrystallizationCrystallography, X-RayProton-Translocating ATPasesPyrococcus horikoshii

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

15272184

Citation

Maegawa, Yuki, et al. "Crystallization and Preliminary X-ray Diffraction Study of the Catalytic Subunit of Archaeal H+ -transporting ATP Synthase From Pyrococcus Horikoshii OT3." Acta Crystallographica. Section D, Biological Crystallography, vol. 60, no. Pt 8, 2004, pp. 1484-6.
Maegawa Y, Morita H, Yao M, et al. Crystallization and preliminary X-ray diffraction study of the catalytic subunit of archaeal H+ -transporting ATP synthase from Pyrococcus horikoshii OT3. Acta Crystallogr D Biol Crystallogr. 2004;60(Pt 8):1484-6.
Maegawa, Y., Morita, H., Yao, M., Watanabe, N., & Tanaka, I. (2004). Crystallization and preliminary X-ray diffraction study of the catalytic subunit of archaeal H+ -transporting ATP synthase from Pyrococcus horikoshii OT3. Acta Crystallographica. Section D, Biological Crystallography, 60(Pt 8), 1484-6.
Maegawa Y, et al. Crystallization and Preliminary X-ray Diffraction Study of the Catalytic Subunit of Archaeal H+ -transporting ATP Synthase From Pyrococcus Horikoshii OT3. Acta Crystallogr D Biol Crystallogr. 2004;60(Pt 8):1484-6. PubMed PMID: 15272184.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Crystallization and preliminary X-ray diffraction study of the catalytic subunit of archaeal H+ -transporting ATP synthase from Pyrococcus horikoshii OT3. AU - Maegawa,Yuki, AU - Morita,Haduki, AU - Yao,Min, AU - Watanabe,Nobuhisa, AU - Tanaka,Isao, Y1 - 2004/07/21/ PY - 2004/05/06/received PY - 2004/06/11/accepted PY - 2004/7/24/pubmed PY - 2005/2/19/medline PY - 2004/7/24/entrez SP - 1484 EP - 6 JF - Acta crystallographica. Section D, Biological crystallography JO - Acta Crystallogr D Biol Crystallogr VL - 60 IS - Pt 8 N2 - H+ -transporting ATP synthase (H+ -ATPase) is a multi-subunit complex which acts to produce ATP molecules. The catalytic subunit A of the archaeal-type H+ -ATPase from Pyrococcus horikoshii OT3 was cloned, expressed in Escherichia coli, purified and crystallized by the hanging-drop vapour-diffusion method with MPD as a precipitant. X-ray intensity data were collected to 2.55 A resolution at beamline BL41XU of SPring-8. The crystals belong to the tetragonal space group P4(1)2(1)2 or P4(3)2(1)2, with unit-cell parameters a = b = 128.0, c = 104.7 A, and contain one molecule per asymmetric unit. SN - 0907-4449 UR - https://www.unboundmedicine.com/medline/citation/15272184/Crystallization_and_preliminary_X_ray_diffraction_study_of_the_catalytic_subunit_of_archaeal_H+__transporting_ATP_synthase_from_Pyrococcus_horikoshii_OT3_ DB - PRIME DP - Unbound Medicine ER -