Crystallization and preliminary X-ray studies of flavocetin-A, a platelet glycoprotein Ib-binding protein from the habu snake venom
1999 ◽
Vol 55
(11)
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pp. 1911-1913
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Keyword(s):
X Ray
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Flavocetin-A (FL-A) is a platelet glycoprotein Ib-binding protein, a high molecular mass oligomer (149 kDa) of C-type lectin-like subunits α and β isolated from the habu snake venom. Purified FL-A crystallized in the tetragonal space group I4 with unit-cell dimensions a = b = 121.0, c = 63.2 Å. The crystals diffract to at least 2.4 Å resolution. The structure has been solved by molecular replacement using the crystal structure of factors IX/X-binding protein (PDB code 1ixx) as a search model. The asymmetric unit contains one heterodimer, showing that FL-A is a novel tetradimer (αβ)4 composed of four heterodimers related by a crystallographic fourfold axis.
1999 ◽
Vol 55
(9)
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pp. 1614-1615
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1999 ◽
Vol 55
(2)
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pp. 566-567
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1999 ◽
Vol 55
(2)
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pp. 414-421
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1971 ◽
Vol 29
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pp. 428-429
1992 ◽
Vol 67
(02)
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pp. 252-257
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1981 ◽
Vol 46
(1)
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pp. 6-19
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2015 ◽
Vol 70
(3)
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pp. 183-190
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1998 ◽
Vol 54
(1)
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pp. 90-92
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