NE1406, the first structural representative of PF09410, reveals a lipocalin-like fold with features that suggest involvement in lipid metabolism. In addition, NE1406 provides potential structural templates for two other protein families (PF07143 and PF08622).

Structures of the ligand-binding domain of human peroxisome proliferator-activated receptor δ in complexes with three novel ligands (JKPL38, JKP39 and JK122) were determined. In addition, the structure of a previously reported complex was updated to higher resolution by obtaining better quality crystals.

Structures of the yeast Sec14-like phosphatidylinositol transfer protein Sfh2 in complex with phosphatidylinositol and squalene reveal structural determinants for ligand recognition.

The CIDE domain was initially identified in apoptotic nucleases and now forms a highly conserved family with diverse functions ranging from cell death to lipid metabolism. Based on structural determination of the DREP3 domain, it is suggested that the head-to-tail helical filament structure might be a unified mechanism of CIDE-domain assembly and represents a critical higher-order scaffolding structure that is important for the function of CIDE-domain-containing proteins in DNA fragmentation and lipid-droplet fusion.

Trigonal crystals of FadR from B. halodurans have been obtained. X-ray data were collected to 2.05 Å resolution using synchrotron radiation.

The first structure of a glycerol kinase from the parasite T. cruzi with a bound glycerol molecule is presented.

The X-ray structure of the tetragonal form of apo acyl-CoA-binding protein (ACBP) from the Harderian gland of the South American armadillo Chaetophractus villosus has been solved.

The CIDE-N domain of CIDE-3 was purified and crystallized. The crystals were found to belong to space group P3₂, with unit-cell parameters a = b = 63.35, c = 37.60 Å, γ = 120°. The crystals were obtained at 293 K and diffracted to a resolution of 2.0 Å.

Yeast Sfh3, a Sec14-like phosphatidylinositol-transfer protein with unique functional properties, has been crystallized. X-ray data sets were collected from native and selenomethionine-substituted crystals to 2.2 and 1.93 Å resolution, respectively.

Further understanding of the structure and function of plasma apolipoproteins requires the determination of their high-resolution structures when complexed with lipids. In these studies, the production of homogeneous, biologically active lipoprotein particles of apolipoprotein E complexed with dipalmitoylphosphatidylcholine and their crystallization and X-ray diffraction are demonstrated.