Crystallization and preliminary X-ray analysis of luffaculin, a ribosome-inactivating protein from sponge-gourd seeds.
Luffaculin is a ribosome-inactivating protein. Crystals suitable for X--ray diffraction were first obtained using the hanging-drop vapour-diffusion method. X-ray studies show that the crystals belong to space group C2, with unit-cell parameters a = 89.90, b = 59.82, c = 55.18 A, beta = 120.81 degrees, and have one molecule in the crystallographic asymmetric unit. The crystals diffract X-rays to at least 2.0 A resolution.
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Department of Protein Engineering, Institute of Biophysics, Chinese Academy of Science, 15 Datun Road, Beijing 100101, People's Republic of China.
Yao
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Wu
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Li
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Li
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J
Dong
Y
Y
D000818:Animals; D003460:Crystallization; D018360:Crystallography, X-Ray; D019662:Cucurbitaceae / Q000737:chemistry; D006023:Glycoproteins / Q000737:chemistry*; D010940:Plant Proteins / Q000737:chemistry*; D011817:Rabbits; D054789:Ribosome Inactivating Proteins, Type 1; D012270:Ribosomes / Q000187:drug effects; D012639:Seeds / Q000737:chemistry; D015978:Trichosanthin / Q000737:chemistry
D006023:Glycoproteins; D010940:Plant Proteins; D054789:Ribosome Inactivating Proteins, Type 1; C088243:luffaculin protein, Luffa acutangula; D015978:Trichosanthin