Purification, crystallization and preliminary X-ray analysis of 3-hydroxy-3-methylglutaryl-coenzyme A reductase of Streptococcus pneumoniae.
Class II 3-hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) reductases are potential targets for novel antibiotic development. In order to obtain a precise structural model for use in virtual screening and inhibitor design, HMG-CoA reductase of Streptococcus pneumoniae was cloned, overexpressed and purified to homogeneity using Ni-NTA affinity chromatography. Crystals were obtained using the hanging-drop vapour-diffusion method. A complete data set was collected from a single frozen crystal on a home X-ray source. The crystal diffracted to 2.3 Å resolution and belonged to the orthorhombic space group C222(1), with unit-cell parameters a = 773.4836, b = 90.3055, c = 160.5592 Å, α = β = γ = 90°. Assuming the presence of two molecules in the asymmetric unit, the solvent content was estimated to be 54.1% (V(M) = 2.68 Å(3) Da(-1)).
School of Pharmaceutical Science, Sun Yat-sen University, Guangzhou 510006, People's Republic of China.
Liping
L
Zhang
Lingling
L
Feng
Li
L
Zhou
Jie
J
Gui
Jian
J
Wan
Xiaopeng
X
Hu
D003460:Crystallization; D018360:Crystallography, X-Ray; D006903:Hydroxymethylglutaryl CoA Reductases / Q000737:chemistry* / Q000302:isolation & purification; D013296:Streptococcus pneumoniae / Q000201:enzymology*
D006903:Hydroxymethylglutaryl CoA Reductases