Open AccessCrystallization and preliminary X‐ray diffraction studies of UP1, the two‐RRM domain of hnRNP A1
Author(s) -
Jokan L.,
Dong A.P.,
Mayeda A.,
Krainer A. R.,
Xu R.M.
Publication year - 1997
Publication title -
acta crystallographica section d
Language(s) - English
Resource type - Journals
ISSN - 1399-0047
DOI - 10.1107/s0907444997003326
Subject(s) - crystallography , crystallization , diffraction , rna splicing , chemistry , rna , alternative splicing , biochemistry , physics , messenger rna , gene , organic chemistry , optics
The N‐terminal domain of hnRNP A1 protein, termed UP1, comprises two tandem RNA‐recognition motifs, both of which are necessary for efficient RNA binding and for the alternative splicing activity of hnRNP A1. Recombinant human UPI expressed in E. coli has been crystallized in space group P 2 1 with unit‐cell dimensions a = 37.94, b = 43.98, c = 55.64 Å and β = 93.9°. The unit‐cell volume is consistent with one UP1 molecule per asymmetric unit and a calculated 49% solvent content. The crystal diffraction limit is higher than 1.3 Å, and a data set to 2.0 Å has been collected. Diffraction data from one platinum and two mercury derivatives have also been collected.