Purification, crystallization and preliminary X-ray analysis of the N-terminal domain of NO38, a nucleolar protein from Xenopus laevis.
NO38 is a multidomain protein that belongs to the nucleoplasmin (Np) family. Previous studies have suggested that acidic chaperones such as Np may function as histone-storage platforms. Here, the purification and crystallization of the N-terminal domain of NO38 in two crystal forms is reported. The C2 crystal form diffracts to 1.9 A and contains two pentamers in the asymmetric unit, while the P1 crystals diffract to 1.7 A and contain a non-crystallographic decamer with 522 symmetry. By analogy with Np, the NO38 decamer may represent the active form of this chaperone.
Namboodiri
V M Haridasan
VM
Department of Physiology and Biophysics, Boston University School of Medicine, 700 Albany Street, Boston, Massachusetts 02118-2526, USA.
Schmidt-Zachmann
Marion S
MS
Head
James F
JF
Akey
Christopher W
CW
D000818:Animals; D001665:Binding Sites; D002118:Calcium / Q000737:chemistry; D002466:Cell Nucleolus; D018360:Crystallography, X-Ray; D018076:DNA, Complementary / Q000378:metabolism; D019281:Dimerization; D008274:Magnesium / Q000737:chemistry; D008958:Models, Molecular; D009687:Nuclear Proteins / Q000737:chemistry* / Q000302:isolation & purification*; D000090243:Nucleophosmin; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D014961:X-Ray Diffraction; D014982:Xenopus laevis
D018076:DNA, Complementary; D009687:Nuclear Proteins; D000090243:Nucleophosmin; D008274:Magnesium; D002118:Calcium