pISSN 2288-6982
eISSN 2288-7105




BioDesign 2021; 9(2): 36-40

Published online June 30, 2021

© Korean Society for Structural Biology

Purification, crystallization, and X-ray crystallographic analysis of spermidine synthase from Kluyveromyces lactis

Seongjin Kim1, Giang Thu Nguyen2 and Jeong Ho Chang1,2,*

1Department of Biology Education, Kyungpook National University, Daegu 41566, Republic of Korea
2Department of Biomedical Convergence Science and Technology, Kyungpook National University, Daegu 41566, Republic of Korea

Correspondence to: *

Received: May 25, 2021; Revised: June 15, 2021; Accepted: June 16, 2021


Spermidine synthase (SpdS) is an aminopropyltransferase that transfers an aminopropyl moiety from decarboxylated S-adenosylmethionine to a variety of polyamines. SpdS enzymes convert putrescine to spermidine and its byproduct methylthioadenosine. In this study, we have overexpressed an N-terminal His6-tagged SpdS from the fungal species Kluyveromyces lactis; it was overexpressed, purified and crystallized to obtain X-ray diffraction data at a high resolution of 1.9 Å. The K. lactis SpdS crystal belongs to the space group P212121 with the following unit cell parameters: a = 65.252 Å, b = 98.180 Å, c = 102.134 Å, and α = β = γ = 90°. There are two molecules in the asymmetric unit.

Graphical Abstract