Crystallization and preliminary X-ray diffraction studies of UP1, the two-RRM domain of hnRNP A1

Jokhan, L., Dong, A. P., Mayeda, A., Krainer, A. R., Xu, R. M. (1997) Crystallization and preliminary X-ray diffraction studies of UP1, the two-RRM domain of hnRNP A1. Acta Crystallographica Section D-Biological Crystallography, 53. pp. 615-618. ISSN 0907-4449

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URL: http://www.ncbi.nlm.nih.gov/pubmed/15299896
DOI: 10.1107/S0907444997003326

Abstract

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 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 consistent with one UP1 molecule per asymmetric unit and a calculated 49% solvent content. The crystal diffraction limit is higher than 1.3 Angstrom, and a data set to 2.0 Angstrom has been collected. Diffraction data from one platinum and two mercury derivatives have also been collected.

Item Type: Paper
Uncontrolled Keywords: rna-binding domain heterogeneous nuclear ribonucleoprotein-a1 heteronuclear magnetic-resonance complex protein-a1 annealing activity splicing factors calf thymus c-proteins spectroscopy specificity
Subjects: bioinformatics > genomics and proteomics > genetics & nucleic acid processing > DNA, RNA structure, function, modification
bioinformatics > genomics and proteomics > genetics & nucleic acid processing
Investigative techniques and equipment > spectroscopy > magnetic resonance spectroscopy
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > DNA, RNA structure, function, modification > nuclear ribonucleoprotein
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > RNA binding protein
Investigative techniques and equipment > spectroscopy
CSHL Authors:
Communities: CSHL labs > Krainer lab
CSHL labs > Xu lab
Depositing User: Matt Covey
Date Deposited: 11 Dec 2013 16:24
Last Modified: 11 Dec 2013 16:24
Related URLs:
URI: http://repository.cshl.edu/id/eprint/28939

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