Leucine-rich-alpha-2-glycoprotein1 (LRG1), a serum protein produced by hepatocytes, functions as a modulator of transforming growth factor beta1 (TGFβ1) signaling in angiogenesis and tumor progression. However, structural studies of LRG1 and detailed binding partner’s interactions have not been reported. To understand structural features and functions of LRG1, purification and crystallization of full length LRG1 were performed in the present study. The crystal of LRG1 diffracted X-rays at a resolution of 2.5 Å. The crystal belonged to space group P6322, having unit cell parameters of a = 143.02 Å, b = 143.02 Å, c = 113.73 Å, α = β = 90º, and γ = 120º with five LRG1 molecules present in the asymmetric unit.
INTRODUCTION
RESULTS AND DISCUSSION
MATERIALS AND METHODS
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