Open AccessCrystallization and preliminary X‐ray analysis of enoyl‐acyl carrier protein reductase (FabK) from Streptococcus pneumoniae
Author(s) -
Saito Jun,
Yamada Mototsugu,
Watanabe Takashi,
Kitagawa Hideo,
Takeuchi Yasuo
Publication year - 2006
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309106017039
Subject(s) - orthorhombic crystal system , crystallization , reductase , acyl carrier protein , streptococcus pneumoniae , resolution (logic) , crystallography , biosynthesis , solvent , chemistry , crystal structure , biochemistry , enzyme , organic chemistry , artificial intelligence , computer science , antibiotics
The enoyl‐acyl carrier protein (ACP) reductase from Streptococcus pneumoniae (FabK; EC 1.3.1.9) is responsible for catalyzing the final step in each elongation cycle of fatty‐acid biosynthesis. Selenomethionine‐substituted FabK was purified and crystallized by the hanging‐drop vapour‐diffusion method at 277 K. The crystal belongs to space group P 2 1 , with unit‐cell parameters a = 50.26, b = 126.70, c = 53.63 Å, β = 112.46°. Diffraction data were collected to 2.00 Å resolution using synchrotron beamline BL32B2 at SPring‐8. Two molecules were estimated to be present in the asymmetric unit, with a solvent content of 45.1%.