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Crystallization and preliminary crystallographic analysis of an acylphosphatase from the hyperthermophilic archaeon Pyrococcus horikoshii.
Acta Crystallogr D Biol Crystallogr. 2004 Jul; 60(Pt 7):1308-10.AC

Abstract

Acylphosphatases catalyse the hydrolysis of the carboxyl phosphate bond in metabolites such as acetyl phosphate, 1,3-bisphosphoglycerate, succinoyl phosphate and carbamoyl phosphate. In this study, acylphosphatase (91 residues) from the hyperthermophilic archaeon Pyrococcus horikoshii has been cloned, overexpressed, purified and crystallized using the sitting-drop vapour-diffusion method using sodium formate as a precipitant at 289 K. The crystals belong to space group P3(2)21, with unit-cell parameters a = b = 85.65, c = 75.51 A. The asymmetric unit contains two molecules of acylphosphatase, with a corresponding crystal volume per protein weight of 3.9 A Da(-1) and a solvent content of 68.6%. A data set diffracting to 1.6 A resolution was collected from a single crystal at 100 K.

Authors+Show Affiliations

Cheung YY
Department of Biochemistry, The Chinese University of Hong Kong, Hong Kong.
Allen MD
No affiliation info available
Bycroft M
No affiliation info available
Wong KB
No affiliation info available

MeSH

Acid Anhydride HydrolasesAmino Acid SequenceAnimalsCrystallizationCrystallography, X-RayMolecular Sequence DataPyrococcus horikoshiiSequence Alignment

Pub Type(s)

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

Language

eng

PubMed ID

15213401

Citation

Cheung, Yuk-Yin, et al. "Crystallization and Preliminary Crystallographic Analysis of an Acylphosphatase From the Hyperthermophilic Archaeon Pyrococcus Horikoshii." Acta Crystallographica. Section D, Biological Crystallography, vol. 60, no. Pt 7, 2004, pp. 1308-10.
Cheung YY, Allen MD, Bycroft M, et al. Crystallization and preliminary crystallographic analysis of an acylphosphatase from the hyperthermophilic archaeon Pyrococcus horikoshii. Acta Crystallogr D Biol Crystallogr. 2004;60(Pt 7):1308-10.
Cheung, Y. Y., Allen, M. D., Bycroft, M., & Wong, K. B. (2004). Crystallization and preliminary crystallographic analysis of an acylphosphatase from the hyperthermophilic archaeon Pyrococcus horikoshii. Acta Crystallographica. Section D, Biological Crystallography, 60(Pt 7), 1308-10.
Cheung YY, et al. Crystallization and Preliminary Crystallographic Analysis of an Acylphosphatase From the Hyperthermophilic Archaeon Pyrococcus Horikoshii. Acta Crystallogr D Biol Crystallogr. 2004;60(Pt 7):1308-10. PubMed PMID: 15213401.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Crystallization and preliminary crystallographic analysis of an acylphosphatase from the hyperthermophilic archaeon Pyrococcus horikoshii. AU - Cheung,Yuk-Yin, AU - Allen,Mark D, AU - Bycroft,Mark, AU - Wong,Kam-Bo, Y1 - 2004/06/22/ PY - 2004/03/24/received PY - 2004/05/05/accepted PY - 2004/6/24/pubmed PY - 2005/3/9/medline PY - 2004/6/24/entrez SP - 1308 EP - 10 JF - Acta crystallographica. Section D, Biological crystallography JO - Acta Crystallogr D Biol Crystallogr VL - 60 IS - Pt 7 N2 - Acylphosphatases catalyse the hydrolysis of the carboxyl phosphate bond in metabolites such as acetyl phosphate, 1,3-bisphosphoglycerate, succinoyl phosphate and carbamoyl phosphate. In this study, acylphosphatase (91 residues) from the hyperthermophilic archaeon Pyrococcus horikoshii has been cloned, overexpressed, purified and crystallized using the sitting-drop vapour-diffusion method using sodium formate as a precipitant at 289 K. The crystals belong to space group P3(2)21, with unit-cell parameters a = b = 85.65, c = 75.51 A. The asymmetric unit contains two molecules of acylphosphatase, with a corresponding crystal volume per protein weight of 3.9 A Da(-1) and a solvent content of 68.6%. A data set diffracting to 1.6 A resolution was collected from a single crystal at 100 K. SN - 0907-4449 UR - https://www.unboundmedicine.com/medline/citation/15213401/Crystallization_and_preliminary_crystallographic_analysis_of_an_acylphosphatase_from_the_hyperthermophilic_archaeon_Pyrococcus_horikoshii_ DB - PRIME DP - Unbound Medicine ER -