TY - JOUR
T1 - Crystallization and preliminary X-ray diffraction studies of UP1, the two-RRM domain of hnRNP A1
AU - Jokhan, Lana
AU - Dong, Ai Ping
AU - Mayeda, Akila
AU - Krainer, Adrian R.
AU - Xu, Rui Ming
PY - 1997
Y1 - 1997
N2 - 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 UP1 expressed in E. coli has been crystallized in space group P21 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.
AB - 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 UP1 expressed in E. coli has been crystallized in space group P21 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.
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U2 - 10.1107/S0907444997003326
DO - 10.1107/S0907444997003326
M3 - Article
C2 - 15299896
AN - SCOPUS:0030886755
SN - 0907-4449
VL - 53
SP - 615
EP - 618
JO - Acta Crystallographica Section D: Biological Crystallography
JF - Acta Crystallographica Section D: Biological Crystallography
IS - 5
ER -