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. 1996 Sep;5(9):1928–1930. doi: 10.1002/pro.5560050920

Purification and crystallization of cyclin-dependent kinase inhibitor p21.

D R Mayrose 1, M A Nichols 1, Y Xiong 1, H Ke 1
PMCID: PMC2143532  PMID: 8880918

Abstract

p21, a universal inhibitor of mammalian cyclin-dependent kinases (CDK), regulates cell cycle progression by forming various distinct protein complexes with cyclins, CDKs, and the proliferating cell nuclear antigen. We have overexpressed recombinant human p21 in E. coli and purified active p21 to near homogeneity on a large scale. Crystals of recombinant p21 have been grown in the space group P2(1) a = 157.4, b = 152.7, c = 90.6 A, and beta = 92.7 degrees. The diffraction data of the recombinant p21 have been collected to 2.5 and 3.5 A resolution for the native crystal and two heavy atom derivatives of mercury and iridium.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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