Crystallization and preliminary crystallographic studies of trichomaglin, novel ribosome-inactivating protein

Authors
Wu, J Gan, JH Xia, ZX
Citation
J. Wu et al., Crystallization and preliminary crystallographic studies of trichomaglin, novel ribosome-inactivating protein, ACT CRYST D, 56, 2000, pp. 1466-1467
Citations number
10
Categorie Soggetti
Chemistry & Analysis
Journal title
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
ISSN journal
09074449 → ACNP
Volume
56
Year of publication
2000
Part
11
Pages
1466 - 1467
Database
ISI
SICI code
0907-4449(200011)56:<1466:CAPCSO>2.0.ZU;2-D
Abstract
Trichomaglin, a novel ribosome-inactivating protein, has been crystallized in two crystal forms using the hanging-drop vapour-diffusion method. The fo rm A and form B crystals belong to the orthorhombic space group P2(1)2(1)2( 1) and the hexagonal space group P6(1) (or P6(5)), respectively. X-ray data have been collected to 3.3 and 2.2 Angstrom resolution for the form A and B crystals, respectively.