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Crystallization and preliminary X‐ray investigation of recombinant human interleukin 10
Author(s) -
Cook William J.,
Windsor William T.,
Murgolo Nicholas J.,
Tindall Stephen H.,
Nagabhushan Tattanahalli L.,
Walter Mark R.
Publication year - 1995
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.340220211
Subject(s) - recombinant dna , crystallization , materials science , chemistry , chemical engineering , engineering , biochemistry , gene
Crystals of recombinant human interleukin 10 have been grown from solutions of ammonium sulfate. The crystals are tetragonal, space group P 4 1 2 1 2 or P 4 3 2 1 2; the unit cell axes are a = 36.5 Å and c = 221.9 Å. There is the equivalent of one polypeptide chain in the asymmetric unit. The crystals are stable to X‐rays and diffract to at least 2.5 Å resolution. © 1995 Wiley‐Liss, Inc.