Crystallization and preliminary X-ray analysis of luffaculin, a ribosome-inactivating protein from sponge-gourd seeds

Authors
Ma, QJ Yao, G Wu, S Li, HJ Li, JH Dong, YC
Citation
Qj. Ma et al., Crystallization and preliminary X-ray analysis of luffaculin, a ribosome-inactivating protein from sponge-gourd seeds, ACT CRYST D, 56, 2000, pp. 185-186
Citations number
12
Categorie Soggetti
Chemistry & Analysis
Journal title
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
ISSN journal
09074449 → ACNP
Volume
56
Year of publication
2000
Part
2
Pages
185 - 186
Database
ISI
SICI code
0907-4449(200002)56:<185:CAPXAO>2.0.ZU;2-Q
Abstract
Luffaculin is a ribosome-inactivating protein. Crystals suitable for X-ray diffraction were first obtained using the hanging-drop vapour-diffusion met hod. X-ray studies show that the crystals belong to space group C2, with un it-cell parameters a = 89.90, b = 59.82, c = 55.18 Angstrom, beta = 120.81 degrees, and have one molecule in the crystallographic asymmetric unit. The crystals diffract X-rays to at least 2.0 Angstrom resolution.