Crystallization and preliminary X-ray diffraction studies of UP1, the two-RRM domain of hnRNP A1.
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 P2(1) with unit-cell dimensions a = 37.94, b = 43.98, c = 55.64 A and beta = 93.9 degrees. 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 A, and a data set to 2.0 A has been collected. Diffraction data from one platinum and two mercury derivatives have also been collected.
Jokan
L
L
W. M. Keck Structural Biology Laboratory, Cold Spring Harbor, NY 11724, USA.
Dong
A P
AP
Mayeda
A
A
Krainer
A R
AR
Xu
R M
RM