Acta Crystallographica Section F

Structural Biology and Crystallization Communications

Volume 61, Part 12 (December 2005)

crystallization communications

Acta Cryst. (2005). F61, 1075-1077 [ doi:10.1107/S1744309105036766 ]

Purification, crystallization and preliminary X-ray crystallographic study of the L-fuculose-1-phosphate aldolase (FucA) from Thermus thermophilus HB8

J. Jeyakanthan, J. Taka, A. Kikuchi, C. Kuroishi, K. Yutani and Y. Shiro

Abstract: Fuculose phosphate aldolase catalyzes the reversible cleavage of L-fuculose-1-phosphate to dihydroxyacetone phosphate and L-lactaldehyde. The protein from Thermus thermophilus HB8 is a biological tetramer with a subunit molecular weight of 21 591 Da. Purified FucA has been crystallized using sitting-drop vapour-diffusion and microbatch techniques at 293 K. The crystals belong to space group P4, with unit-cell parameters a = b = 100.94, c = 45.87 Å. The presence of a dimer of the enzyme in the asymmetric unit was estimated to give a Matthews coefficient (V_M) of 2.7 Å³ Da^-1 and a solvent content of 54.2%(v/v). Three-wavelength diffraction MAD data were collected to 2.3 Å from zinc-containing crystals. Native diffraction data to 1.9 Å resolution have been collected using synchrotron radiation at SPring-8.

Keywords: fuculose phosphate aldolase; class II aldolases; Thermus thermophilus HB8.