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Cloning, purification, crystallization and preliminary crystallographic analysis of acylphosphatase from Pyrococcus horikoshii OT3.
Acta Crystallogr D Biol Crystallogr. 2004 Jun; 60(Pt 6):1135-6.AC

Abstract

Acylphosphatase is one of the smallest enzymes and catalyzes the hydrolysis of the carboxy-phosphate bond. An extremely thermostable acylphosphatase from a hyperthermophilic archaea, Pyrococcus horikoshii OT3, has been cloned, expressed in Escherichia coli, purified and crystallized using the sitting-drop vapour-diffusion method with potassium/sodium tartrate as the precipitant at pH 5.5. X-ray diffraction data have been collected to a highest resolution of 1.72 angstroms on a synchrotron-radiation source. The crystals belong to space group P3(2)21, with approximate unit-cell parameters a = b = 86.6, c = 75.4 angstroms and two monomers in the asymmetric unit.

Authors+Show Affiliations

Miyazono KI
Department of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-8657, Japan.
Kudo N
No affiliation info available
Tanokura M
No affiliation info available

MeSH

Acid Anhydride HydrolasesCarbonCloning, MolecularCrystallizationCrystallography, X-RayDiffusionEscherichia coliHydrogen-Ion ConcentrationModels, StatisticalPhosphatesPyrococcus horikoshiiSynchrotronsTartratesX-Ray Diffraction

Pub Type(s)

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

Language

eng

PubMed ID

15159579

Citation

Miyazono, Ken Ichi, et al. "Cloning, Purification, Crystallization and Preliminary Crystallographic Analysis of Acylphosphatase From Pyrococcus Horikoshii OT3." Acta Crystallographica. Section D, Biological Crystallography, vol. 60, no. Pt 6, 2004, pp. 1135-6.
Miyazono KI, Kudo N, Tanokura M. Cloning, purification, crystallization and preliminary crystallographic analysis of acylphosphatase from Pyrococcus horikoshii OT3. Acta Crystallogr D Biol Crystallogr. 2004;60(Pt 6):1135-6.
Miyazono, K. I., Kudo, N., & Tanokura, M. (2004). Cloning, purification, crystallization and preliminary crystallographic analysis of acylphosphatase from Pyrococcus horikoshii OT3. Acta Crystallographica. Section D, Biological Crystallography, 60(Pt 6), 1135-6.
Miyazono KI, Kudo N, Tanokura M. Cloning, Purification, Crystallization and Preliminary Crystallographic Analysis of Acylphosphatase From Pyrococcus Horikoshii OT3. Acta Crystallogr D Biol Crystallogr. 2004;60(Pt 6):1135-6. PubMed PMID: 15159579.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Cloning, purification, crystallization and preliminary crystallographic analysis of acylphosphatase from Pyrococcus horikoshii OT3. AU - Miyazono,Ken Ichi, AU - Kudo,Norio, AU - Tanokura,Masaru, Y1 - 2004/05/21/ PY - 2004/03/09/received PY - 2004/03/31/accepted PY - 2004/5/26/pubmed PY - 2005/2/3/medline PY - 2004/5/26/entrez SP - 1135 EP - 6 JF - Acta crystallographica. Section D, Biological crystallography JO - Acta Crystallogr D Biol Crystallogr VL - 60 IS - Pt 6 N2 - Acylphosphatase is one of the smallest enzymes and catalyzes the hydrolysis of the carboxy-phosphate bond. An extremely thermostable acylphosphatase from a hyperthermophilic archaea, Pyrococcus horikoshii OT3, has been cloned, expressed in Escherichia coli, purified and crystallized using the sitting-drop vapour-diffusion method with potassium/sodium tartrate as the precipitant at pH 5.5. X-ray diffraction data have been collected to a highest resolution of 1.72 angstroms on a synchrotron-radiation source. The crystals belong to space group P3(2)21, with approximate unit-cell parameters a = b = 86.6, c = 75.4 angstroms and two monomers in the asymmetric unit. SN - 0907-4449 UR - https://www.unboundmedicine.com/medline/citation/15159579/Cloning_purification_crystallization_and_preliminary_crystallographic_analysis_of_acylphosphatase_from_Pyrococcus_horikoshii_OT3_ DB - PRIME DP - Unbound Medicine ER -