Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.

Science 19 February 1971:
Vol. 171. no. 3972, pp. 677 - 680
DOI: 10.1126/science.171.3972.677
Prev | Table of Contents | Next

Articles

Subunit Structure of Aldolase

Elizabeth G. Heidner 1, Bruce H. Weber 2, and David Eisenberg 2

1 Department of Chemistry and Molecular Biology Institute, University of California,Los Angeles 90024
2 Department of Chemistry and Molecular Biology Institute, University of California, Los Angeles 90024

A new crystal form of rabbit muscle aldolase shows that the molecule has 222 symmetry to at least 4-angstrom resolution, and hence that the gross conformation of the four subunits is the same. Comparison of the new form with a previously reported form establishes the number of molecules per unit cell, n, in the older form. For an independent check, the "crystal-volume and protein-content method" was developed to determine n without directly measuring the water content of the crystals.

To Advertise     Find Products

Science. ISSN 0036-8075 (print), 1095-9203 (online)