Crystallization and crystallographic investigations of the small subunit of mouse ribonucleotide reductase.

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 Lett

journal_title

FEBS letters

authors

Nielsen BB,Kauppi B,Thelander M,Thelander L,Larsen IK,Eklund H

doi

10.1016/0014-5793(95)01067-o

subject

Has Abstract

pub_date

1995-10-16 00:00:00

pages

310-2

issue

3

eissn

0014-5793

issn

1873-3468

pii

0014-5793(95)01067-O

journal_volume

373

pub_type

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