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XB-ART-2628
Acta Crystallogr D Biol Crystallogr 2004 Dec 01;60Pt 12 Pt 2:2325-7. doi: 10.1107/S0907444904023959.
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Purification, crystallization and preliminary X-ray analysis of the N-terminal domain of NO38, a nucleolar protein from Xenopus laevis.

Namboodiri VM , Schmidt-Zachmann MS , Head JF , Akey CW .


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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.

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Species referenced: Xenopus laevis
Genes referenced: npm1