Crystallization and preliminary X-ray diffraction study of fructan 1-exohydrolase IIa from Cichorium intybus

• Published in: Acta crystallographica. Section D, Biological crystallography. Vol. 60; no. 3; pp. 553 - 554
• Main Authors: Verhaest, Maureen, Van den Ende, Wim, Yoshida, Midori, Le Roy, Katrien, Peeraer, Yves, Sansen, Stefaan, De Ranter, Camiel J., Van Laere, André, Rabijns, Anja
• Format: Journal Article
• Language: English
• Published: 5 Abbey Square, Chester, Cheshire CH1 2HU, England International Union of Crystallography 01.03.2004
• Subjects: Cichorium intybus - enzymology; Crystallization; Crystallography, X-Ray; fructan degradation; fructan exohydrolase; Fructans - metabolism; Glycoside Hydrolases - chemistry; Glycoside Hydrolases - metabolism; Plant Proteins - chemistry; Plant Proteins - metabolism
• ISSN: 1399-0047; 0907-4449; 1399-0047
• DOI: 10.1107/S0907444903029317

Fructan 1‐exohydrolase IIa (1‐FEH IIa), a plant enzyme involved in fructan breakdown, has been crystallized using the hanging‐drop vapour‐diffusion method at 277 K. The crystals are tetragonal, belonging to space group P41212 or P43212, with unit‐cell parameters a = 139.83, b = 139.83, c = 181.94 Å. Calculation of the Matthews coefficient indicates there to be two or three molecules in the asymmetric unit. Synchrotron radiation was used to collect a complete native data set to a resolution of 2.35 Å.