Crystallization and preliminary X-ray analysis of recombinant bovine cellular retinoic acid-binding protein.
1994 (engelsk)Inngår i: Acta Crystallogr D Biol Crystallogr, ISSN 0907-4449, Vol. 50, nr Pt 4, s. 370-4Artikkel i tidsskrift (Fagfellevurdert) Published
Abstract [en]
Crystals of bovine cellular retinoic acid-binding protein (CRABPI) have been grown from protein expressed in E. coli. Two different crystal forms were obtained. Crystals containing protein with the ligand all-trans retinoic acid belong to space group P4(1) or P4(3), a = b = 41.36, c = 202.71 A and diffract to 2.5 A. Crystals of CRABP with the synthetic retinoid analogue Am80 diffract to 1.9 A with space group P2(1) and cell dimensions a = 37.03, b = 105.93, c = 40.31 A, beta = 110.28 degrees. Considerations in the crystallization of proteins with light-sensitive ligands are discussed.
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1994. Vol. 50, nr Pt 4, s. 370-4
Identifikatorer
URN: urn:nbn:se:uu:diva-21225PubMedID: 15299387OAI: oai:DiVA.org:uu-21225DiVA, id: diva2:48998
2006-12-152006-12-152011-01-16