Crystallization and preliminary X-ray investigation of recombinant human interleukin 10

Crystals of recombinant human interleukin 10 have been grown from solutions of ammonium sulfate. The crystals are tetragonal, space group P41212 or P43212; 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 sta...

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Veröffentlicht in:	Proteins, structure, function, and bioinformatics structure, function, and bioinformatics, 1995-06, Vol.22 (2), p.187-190
Hauptverfasser:	Cook, William J., Windsor, William T., Murgolo, Nicholas J., Tindall, Stephen H., Nagabhushan, Tattanahalli L., Walter, Mark R.
Format:	Artikel
Sprache:	eng
Schlagworte:	Ammonium Sulfate - chemistry Animals BCRF1 CHO Cells - metabolism Cricetinae crystal seeding cytokine Escherichia coli - metabolism Humans Interleukin-10 - chemistry protein structure Recombinant Proteins - biosynthesis Recombinant Proteins - chemistry X-Ray Diffraction
Online-Zugang:	Volltext
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Zusammenfassung:	Crystals of recombinant human interleukin 10 have been grown from solutions of ammonium sulfate. The crystals are tetragonal, space group P41212 or P43212; 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.
ISSN:	0887-3585 1097-0134
DOI:	10.1002/prot.340220211