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Initial crystallographic analysis of a recombinant human interleukin-1 receptor antagonist protein (1994)

Clancy, L. L. ; Finzel, B. C. ; Yem, A. W. ; [et al.]

Copenhagen : International Union of Crystallography (IUCr)

Acta crystallographica 50 (1994), S. 197-201

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ISSN: 1399-0047

Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001

Topics: Chemistry and Pharmacology , Geosciences , Physics

Notes: 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 P43212 and unit-cell dimensions of a = b = 72.35(26), c = 114.7(8) Å and Z = 16 (two molecules per asymmetric unit). Fresh crystals diffract to about 2.3 Å 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 Å resolution calculated with these derivatives confirms that the IRAP molecule is a member of the interleukin-1 structural family.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1107/S0907444993009394

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Crystallization of purified recombinant human interleukin-1β (1988)

Carter, D. B. ; Curry, K. A. ; Tomich, C-S. C. ; [et al.]

New York, NY : Wiley-Blackwell

Proteins: Structure, Function, and Genetics 3 (1988), S. 121-129

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ISSN: 0887-3585

Keywords: bioactivity ; SK-hep-1 hepatoma ; interleukin-1 ; recombinant protein ; crystals ; Chemistry ; Biochemistry and Biotechnology

Source: Wiley InterScience Backfile Collection 1832-2000

Topics: Medicine

Notes: The gene for human interleukin-1β was cloned from SK-hep-1 hepatoma cellular RNA and expressed at high levels in Escherichia coli both as the naturally processed form (rIL-1β) and as a variant with an additional sequence of three amino acids on the N-terminus (rIL-1β+). Expressed protein was purified to homogeneity by a sequence of steps, which included low pH incubation, adsorption and desorption from Procion Red Sepharose, sizing on a Superose 12 fast-performance liquid chromatography (FPLC) column, and anion exchange chromatography on QAE Sepharose. The final step provided a biologically active protein that migrates on twodimensional (2-D) gels as a single spot with a pI of 6.7 ± 0.2 and a molecular mass of 17,500 daltons. Concentrated solutions of rIL-1β have produced crystals by ammonium sulfate precipitation. The crystals are tetragonal, show the symmetry of space group P41 or its enantiomer, have lattice constants of a = 58.46 (1) and c = 77.02 (3) A, and scatter to at least 2 Å resolution. A structure determination based on these crystals is under way.

Additional Material: 6 Ill.