CRYSTALLIZATION AND PRELIMINARY-X-RAY DIFFRACTION STUDIES OF UP1, THE2-RRM DOMAIN OF HNRNP A1

The N-terminal domain of hnRNP A1 protein, termed UP1, comprises two t andem RNA-recognition motifs, both of which are necessary for efficien t RNA binding and for the alternative splicing activity of hnRNP A1. R ecombinant human UP1 expressed in E. coli has been crystallized in spa ce group P2(1) with unit-cell dimensions a = 37.94, b = 43.98, c = 55. 64 Angstrom and beta = 93.9 degrees. The unit-cell volume is consisten t with one UP1 molecule per asymmetric unit and a calculated 49% solve nt content. The crystal diffraction limit is higher than 1.3 Angstrom, and a data set to 2.0 Angstrom has been collected. Diffraction data f rom one platinum and two mercury derivatives have also been collected.