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2irt
From Proteopedia
INITIAL CRYSTALLOGRAPHIC ANALYSES OF A RECOMBINANT INTERLEUKIN-1 RECEPTOR ANTAGONIST PROTEIN
Overview
We report the crystallization of samples of a recombinant preparation of human interleukin-1 receptor antagonist protein (IRAP) and solution of the crystal structure by isomorphous replacement methods. Crystals were obtained by the hanging-drop vapor-diffusion method at 277 K from solutions of PEG 4000 containing sodium chloride, dithiothreitol and PIPES [sodium piperazione-N,N'-bis(2-ethanesulfonate)] buffer at pH 7.0. Crystals appear within about a week and grow as truncated tetragonal bipyramids to 0.3-0.6 mm on an edge. X-ray diffraction data from these crystals specify space group P4(3)2(1)2 and unit-cell dimensions of a = b = 72.35(26), c = 114.7(8) A and Z = 16 (two molecules per asymmetric unit). Fresh crystals diffract to about 2.3 A resolution. The search for heavy-atom derivatives has produced two, potassium gold cyanide and trimethyl lead chloride, as same-site, single-site derivatives. Inspection of an electron-density map at 4 A resolution calculated with these derivatives confirms that the IRAP molecule is a member of the interleukin-1 structural family.
About this Structure
2IRT is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Initial crystallographic analysis of a recombinant human interleukin-1 receptor antagonist protein., Clancy LL, Finzel BC, Yem AW, Deibel MR Jr, Strakalaitis NA, Brunner DP, Sweet RM, Einspahr HM, Acta Crystallogr D Biol Crystallogr. 1994 Mar 1;50(Pt 2):197-201. PMID:15299459 Page seeded by OCA on Sun May 4 07:47:21 2008
