Cold-active beta-galactosidase from Arthrobacter sp. C2-2 forms compact 660 kDa hexamers: crystal structure at 1.9A resolution.
Skálová, Tereza
Cold-active beta-galactosidase from Arthrobacter sp. C2-2 forms compact 660 kDa hexamers: crystal structure at 1.9A resolution. [electronic resource] - Journal of molecular biology Oct 2005 - 282-94 p. digital
Publication Type: Journal Article; Research Support, Non-U.S. Gov't
0022-2836
10.1016/j.jmb.2005.08.028 doi
Amino Acid Sequence
Arthrobacter--enzymology
Bacterial Proteins--chemistry
Binding Sites
Cold Temperature
Crystallography, X-Ray
Humans
Ions--chemistry
Models, Molecular
Molecular Sequence Data
Protein Structure, Quaternary
Sequence Alignment
Solvents--chemistry
beta-Galactosidase--chemistry
Cold-active beta-galactosidase from Arthrobacter sp. C2-2 forms compact 660 kDa hexamers: crystal structure at 1.9A resolution. [electronic resource] - Journal of molecular biology Oct 2005 - 282-94 p. digital
Publication Type: Journal Article; Research Support, Non-U.S. Gov't
0022-2836
10.1016/j.jmb.2005.08.028 doi
Amino Acid Sequence
Arthrobacter--enzymology
Bacterial Proteins--chemistry
Binding Sites
Cold Temperature
Crystallography, X-Ray
Humans
Ions--chemistry
Models, Molecular
Molecular Sequence Data
Protein Structure, Quaternary
Sequence Alignment
Solvents--chemistry
beta-Galactosidase--chemistry