tretinoin and formic-acid

tretinoin has been researched along with formic-acid* in 1 studies

Other Studies

1 other study(ies) available for tretinoin and formic-acid

Article	Year
Purification and crystallization of the heterodimeric complex of RARbeta and RXRalpha ligand-binding domains in the active conformation. Acta crystallographica. Section D, Biological crystallography, 2004, Volume: 60, Issue:Pt 6 The ligand-binding domains of the retinoid X receptor alpha (RXRalpha) and of the retinoic acid receptor beta (RARbeta) were overexpressed separately and copurified in the heterodimeric form. Using a crystallization solution containing sodium formate and PEG 3350 as precipitant, the heterodimer was cocrystallized with the promiscuous ligand 9-cis-retinoic acid (9C-RA) and a 13-residue fragment of the nuclear receptor interaction domain (NID) of the transcriptional coactivator TRAP220. The crystals grew in the trigonal space group P3(1)21, with unit-cell parameters a = b = 115.7, c = 247.2 angstroms and two heterodimers per asymmetric unit. X-ray diffraction data were collected to 2.9 angstroms resolution. The structure was solved by molecular replacement and is currently being refined. Topics: Alitretinoin; Animals; Dimerization; Escherichia coli; Formates; Genetic Vectors; Histidine; Ligands; Mice; Protein Conformation; Protein Structure, Tertiary; Receptors, Retinoic Acid; Retinoic Acid Receptor alpha; Tretinoin; X-Ray Diffraction	2004

Article

Year

Purification and crystallization of the heterodimeric complex of RARbeta and RXRalpha ligand-binding domains in the active conformation.

Acta crystallographica. Section D, Biological crystallography, 2004, Volume: 60, Issue:Pt 6

The ligand-binding domains of the retinoid X receptor alpha (RXRalpha) and of the retinoic acid receptor beta (RARbeta) were overexpressed separately and copurified in the heterodimeric form. Using a crystallization solution containing sodium formate and PEG 3350 as precipitant, the heterodimer was cocrystallized with the promiscuous ligand 9-cis-retinoic acid (9C-RA) and a 13-residue fragment of the nuclear receptor interaction domain (NID) of the transcriptional coactivator TRAP220. The crystals grew in the trigonal space group P3(1)21, with unit-cell parameters a = b = 115.7, c = 247.2 angstroms and two heterodimers per asymmetric unit. X-ray diffraction data were collected to 2.9 angstroms resolution. The structure was solved by molecular replacement and is currently being refined.

Topics: Alitretinoin; Animals; Dimerization; Escherichia coli; Formates; Genetic Vectors; Histidine; Ligands; Mice; Protein Conformation; Protein Structure, Tertiary; Receptors, Retinoic Acid; Retinoic Acid Receptor alpha; Tretinoin; X-Ray Diffraction

2004