L. Loleggio et al., CRYSTALLIZATION AND PRELIMINARY-X-RAY ANALYSIS OF THE MAJOR ENDOGLUCANASE FROM THERMOASCUS-AURANTIACUS, Acta crystallographica. Section D, Biological crystallography, 53, 1997, pp. 599-604
Citations number
19
Categorie Soggetti
Crystallography,"Biochemical Research Methods",Biology
The major endoglucanase (35 kDa) from the thermophilic fungus Thermoas
cus aurantiacus has been purified from culture filtrates using an affi
nity method and the sequence for 35 N-terminal amino acids determined.
This has allowed assignment of the enzyme to subtype A6 of family 5 e
ndoglucanases. The enzyme has been crystallized as thick plates by the
hanging-drop method using ammonium sulfate as precipitant. The crysta
ls belong to space group P2(1)2(1)2(1) with cell edges a = 76.4, b = 8
5.7 and c = 89.5 Angstrom, with two molecules in the asymmetric unit,
and diffract to 1.62 Angstrom resolution using synchrotron radiation.
The structure will be solved by isomorphous replacement.