$Preparation and X-ray crystallographic analysis of recombinant obelin crystals diffracting to beyond 1.1 Å$

Preparation and X-ray crystallographic analysis of recombinant obelin crystals diffracting to beyond 1.1 Å

Crystals of recombinant obelin, the Ca2+‐regulated photoprotein from the marine hydroid Obelia longissima, have been grown from a solution containing PEG 8000 and potassium phosphate. Hexaminecobalt trichloride was used as an additive to increase the chance of crystallization. The crystals grow in a...

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Veröffentlicht in:	Acta crystallographica. Section D, Biological crystallography. Biological crystallography., 2001-12, Vol.57 (12), p.1919-1921
Hauptverfasser:	Vysotski, Eugene S., Liu, Zhi-Jie, Rose, John, Wang, B. C., Lee, John
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Cnidaria - chemistry Crystallization Crystallography, X-Ray Luminescent Proteins - chemistry Luminescent Proteins - isolation & purification obelin photoproteins Protein Conformation Recombinant Proteins - chemistry Recombinant Proteins - isolation & purification
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Zusammenfassung:	Crystals of recombinant obelin, the Ca2+‐regulated photoprotein from the marine hydroid Obelia longissima, have been grown from a solution containing PEG 8000 and potassium phosphate. Hexaminecobalt trichloride was used as an additive to increase the chance of crystallization. The crystals grow in a light yellow cubic form (0.5 × 0.5 × 0.45 mm) which diffracts to beyond 1.1 Å resolution. The crystals belong to the space group C2, with unit‐cell parameters a = 83.43, b = 54.92, c = 52.99 Å, β = 112.00°. The asymmetric unit contains one molecule. Crystals exposed to calcium ion before and after X‐ray irradiation emit light, confirming that the crystals consist of an active photoprotein.
ISSN:	1399-0047 0907-4449 1399-0047
DOI:	10.1107/S0907444901016523