Premium
New crystal forms of the small subunit of ribonucleotide reductase from Escherichia coli
Author(s) -
Nordlund Par,
Uhlin Ulla,
Westergren Christina,
Joelsen Thorleif,
Sjöberg Britt-Marie,
Eklund Hans
Publication year - 1989
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(89)81666-7
Subject(s) - ribonucleotide reductase , orthorhombic crystal system , escherichia coli , protein subunit , crystallography , dimer , ribonucleotide , chemistry , crystal (programming language) , resolution (logic) , stereochemistry , crystal structure , nucleotide , biochemistry , organic chemistry , artificial intelligence , computer science , programming language , gene
The small subunit of ribonucleotide reductase from Escherichia coli has been crystallized in two new crystal forms. The form most suitable for X‐ray analysis belongs to the orthorhombic space group P2 1 2 1 2 1 . It,has the cell dimensions 74.3 Å, 85.5 Å, 115.7 Å and diffracts to about 2.1 Å resolution. The asymmetric unit most probably contains one dimer. Absorption spectra of single crystals confirm that the crystals contain a binuclear iron center. Crystals of the iron‐depleted apoenzyme have also been obtained.