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Crystallization and preliminary crystallographic analysis of an acylphosphatase from the hyperthermophilic archaeon Pyrococcus horikoshii
- Source :
- Acta crystallographica. Section D, Biological crystallography. 60(Pt 7)
- Publication Year :
- 2004
-
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.
- Subjects :
- biology
Sodium formate
Molecular Sequence Data
General Medicine
Phosphate
biology.organism_classification
Acylphosphatase
Crystallography, X-Ray
law.invention
Acid Anhydride Hydrolases
chemistry.chemical_compound
Hydrolysis
Amyloid disease
Crystallography
Pyrococcus horikoshii
chemistry
Structural Biology
law
Carbamoyl phosphate
Animals
Amino Acid Sequence
Crystallization
Sequence Alignment
Subjects
Details
- ISSN :
- 09074449
- Volume :
- 60
- Issue :
- Pt 7
- Database :
- OpenAIRE
- Journal :
- Acta crystallographica. Section D, Biological crystallography
- Accession number :
- edsair.doi.dedup.....fe604d1bf69337c5a0f7b148b2949cd7