CRYSTALLIZATION AND PRELIMINARY-X-RAY ANALYSIS OF A COHESIN DOMAIN OFTHE CELLULOSOME FROM CLOSTRIDIUM-THERMOCELLUM

Authors
SHIMON LJW FROLOW F YARON S BAYER EA LAMED R MORAG E SHOHAM Y
Citation
Ljw. Shimon et al., CRYSTALLIZATION AND PRELIMINARY-X-RAY ANALYSIS OF A COHESIN DOMAIN OFTHE CELLULOSOME FROM CLOSTRIDIUM-THERMOCELLUM, Acta crystallographica. Section D, Biological crystallography, 53, 1997, pp. 114-115
Citations number
15
Categorie Soggetti
Crystallography,"Biochemical Research Methods",Biology
Journal title
Acta crystallographica. Section D, Biological crystallography → ACNP
ISSN journal
09074449
Volume
53
Year of publication
1997
Part
1
Pages
114 - 115
Database
ISI
SICI code
0907-4449(1997)53:<114:CAPAOA>2.0.ZU;2-5
Abstract
Recombinant cohesin-2, a unique type of protein-recognition domain fro m the cellulosome of Clostridium thermocellum, has been crystallized b y tile hanging-drop vapor-diffusion method. The crystals are monoclini c, space group C2 with unit-cell dimensions a = 79.91, b = 47.86, c = 51.13 Angstrom, beta = 126.77 degrees. There is most likely to be one molecule per asymmetric unit, corresponding to a packing density of 2. 16 Angstrom(3) Da(-1). The crystals diffract to beyond 2.3 Angstrom on a conventional laboratory rotating-anode source.