Purification, crystallization and preliminary X-ray crystallographic analysis of nucleoside diphosphate kinase from rice

• Published in: Acta crystallographica. Section D, Biological crystallography. Vol. 59; no. 9; pp. 1648 - 1650
• Main Authors: Huang, Jen-Yen, Chang, Chia-Yu, Chang, Tschining, Chen, Chun-Jung
• Format: Journal Article
• Language: English
• Published: 5 Abbey Square, Chester, Cheshire CH1 2HU, England Munksgaard International Publishers 01.09.2003
• Subjects: Cloning, Molecular - methods; Crystallization - methods; Crystallography, X-Ray; nucleoside diphosphate kinase; Nucleoside-Diphosphate Kinase - chemistry; Nucleoside-Diphosphate Kinase - genetics; Nucleoside-Diphosphate Kinase - isolation & purification; Oryza - enzymology; Plant Proteins - chemistry; Protein Conformation; rice
• DOI: 10.1107/S0907444903014616
• ISSN: 1399-0047; 0907-4449

Nucleoside diphosphate kinase (NDK) catalyses the transfer of the γ‐­phosphoryl group from a nucleoside triphosphate (NTP) to a nucleoside diphosphate (NDP). NDK is involved in and required for coleoptile elongation in rice. The level of the enzyme changes during seed germination and the early stages of seedling growth. Recombinant rice NDK (rNDK) has been crystallized using the hanging‐drop vapour‐diffusion method. rNDK crystals diffracted to a resolution of 2.50 Å and belong to space group P212121, with unit‐cell parameters a = 70.98, b = 182.26, c = 188.30 Å. Preliminary analysis indicates there to be 12 rNDK molecules in each asymmetric unit, with a solvent content of 47.2%.