Crystallization of the calcium-activated phosphoenolpyruvate carboxykinase from Escherichia coli K12

• Published in: Journal of molecular biology Vol. 219; no. 4; pp. 593 - 594
• Main Authors: Delbaere, Louis T.J., Vandonselaar, Margaret, Glaeske, Daniel, Jabs, Corrine, Goldie, Hughes
• Format: Journal Article
• Language: English
• Published: Oxford Elsevier Ltd 20.06.1991; Elsevier
• Subjects: Biological and medical sciences; Calcium - metabolism; calcium-activated; Crystalline structure; Crystallization; enzyme; Escherichia coli - enzymology; Fundamental and applied biological sciences. Psychology; gluconeogenesis; Molecular biophysics; Molecular Structure; Phosphoenolpyruvate Carboxykinase (GTP) - chemistry; Phosphoenolpyruvate Carboxykinase (GTP) - metabolism; reseeding; Structure in molecular biology; X-Ray Diffraction; enzyme; crystallization; calcium-activated; reseeding; gluconeogenesis; Unit cell; Enzyme; Escherichia coli; Crystallization; Bacteria; X ray diffraction; Phosphoenolpyruvate carboxykinase (ATP); Enterobacteriaceae
• ISSN: 0022-2836; 1089-8638
• DOI: 10.1016/0022-2836(91)90654-O

Single crystals of phosphoenolpyruvate carboxykinase from Escherichia coli K12 have been grown in the orthorhombic crystal system. Single crystals developed to a maximum size of 0.25 mm × 0.25 mm × 1.5 mm by the technique of washing and reseeding. The space group is P2 1 2 1 2 1, with a = 77.24 A ̊ , b = 89.18 A ̊ , c = 93.24 A ̊ and Z = 4 ; there is one enzyme molecule per crystallographic asymmetric unit and the solvent content is estimated to be 59%. The crystals diffract to at least 2.8 Å d spacings and decompose in the X-ray beam after approximately two days of exposure.