Hsp90 is a molecular chaperone that promotes protein folding and maturation of various client proteins. In this study, we purified Candida glabrata Hsp90 and crystallized the protein in 100 mM HEPES-NaOH pH7.5, 70% 2-methyl-2,4- pentanediol. We collected the x-ray diffraction data to 1.9 A resolution. The crystals belong to the space group P4322 with unit cell parameters a = b = 73.9 A, and c = 108.7 A. Solvent content analysis suggested that a proteolytic fragment of the full-length formed the crystals. We determined the structure of the ATP-binding N-terminal domain (NTD) by molecular replacement using a structure of S. cerevisiae Hsc82. The asymmetric unit contained one NTD with a solvent content of 59.5%. The structure of CgHsp90 NTD spanning the residues 2-212 was refined to the Rfree factor of 22.7%. The structure reveals an open conformation of the nucleotide-binding site and structural conservation of the NTDs in fungal Hsp90 proteins.