Crystal structure of human alpha-lactalbumin at 1.7 A resolution.
The three-dimensional X-ray structure of human alpha-lactalbumin, an important component of milk, has been determined at 1.7 A (0.17 nm) resolution by the method of molecular replacement, using the refined structure of baboon alpha-lactalbumin as the model structure. The two proteins are known to ha...
Main Authors: | Acharya, K, Ren, J, Stuart, D, Phillips, D, Fenna, R |
---|---|
Format: | Journal article |
Language: | English |
Published: |
1991
|
Similar Items
-
Refined structure of baboon alpha-lactalbumin at 1.7 A resolution. Comparison with C-type lysozyme.
by: Acharya, K, et al.
Published: (1989) -
Crystallographic analysis of the three-dimensional structure of baboon alpha-lactalbumin at low resolution. Homology with lysozyme.
by: Smith, S, et al.
Published: (1987) -
A critical evaluation of the predicted and X-ray structures of alpha-lactalbumin.
by: Acharya, K, et al.
Published: (1990) -
From lysozyme to alpha-lactalbumin: protein engineering and evolution.
by: Phillips, D, et al.
Published: (1987) -
Alpha-lactalbumin possesses a distinct zinc binding site.
by: Ren, J, et al.
Published: (1993)