| Autor: |
Stevens, Fred J., Westholm, Florence A., Panagiotopoulos, Nicolas, Solomon, Alan, Schiffer, Marianne |
| Zdroj: |
ETSU Faculty Works. |
| Druh dokumentu: |
Text |
| DOI: |
10.1016/0022-2836(81)90085-1 |
| Popis: |
A complete human λ Bence Jones protein dimer (Cle) has been isolated and crystallized. Protein Cle was characterized immunochemically and chemically as having a variable region amino acid sequence associated with light chains of the λ chain subgroup, λIII, and a constant region sequence characteristic of "non-Mcg" type λ chains. Bence Jones protein Cle contains two covalently bound intact monomers, each having a molecular weight of ~23,000. Crystals of Bence Jones protein Cle, obtained from ammonium sulfate solutions, diffract to 2.6 Å resolution and have the orthorhombic space group P212121 with cell dimensions a = 113.0 A ̊, b = 72.3 A ̊, and c = 48.9 A ̊. The asymmetric unit consists of a dimer with a molecular weight of ~ 46,000. |
| Databáze: |
Networked Digital Library of Theses & Dissertations |
| Externí odkaz: |
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