Abstract:
:The R2 protein component of mouse ribonucleotide reductase has been obtained from overproducing Escherichia coli bacteria. It has been crystallized using NaCl as precipitant. The crystals are orthorhombic, space group C222(1), with cell dimensions a = 76.9 A, b = 108.9 A, c = 92.7 A and diffract to at least 2.5 A. The asymmetric unit of the crystals contains one monomer. Rotation and translation function searches using a model based on the weakly homologous E. coli R2 gave one significant peak. Rotation about a crystallographic 2-fold axis parallel to the a-axis produces an R2 dimer with dimer interactions very similar to those found for E. coli R2.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Nielsen BB,Kauppi B,Thelander M,Thelander L,Larsen IK,Eklund Hdoi
10.1016/0014-5793(95)01067-osubject
Has Abstractpub_date
1995-10-16 00:00:00pages
310-2issue
3eissn
0014-5793issn
1873-3468pii
0014-5793(95)01067-Ojournal_volume
373pub_type
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