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X-ray Structure of Recombinant Ricin A-Chain at 1.8 Å Resolution

✍ Scribed by Simon A. Weston; Alec D. Tucker; David R. Thatcher; Dean J. Derbyshire; Richard A. Pauptit

Book ID
115626956
Publisher
Elsevier Science
Year
1994
Tongue
English
Weight
890 KB
Volume
244
Category
Article
ISSN
0022-2836

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📜 SIMILAR VOLUMES

Structure of recombinant ricin A chain a
Structure of recombinant ricin A chain at 2.3 Å
✍ Debra Mlsna; Arthur F. Monzingo; Betsy J. Katzin; Stephen Ernst; Jon D. Robertus 📂 Article 📅 2008 🏛 Cold Spring Harbor Laboratory Press 🌐 English ⚖ 565 KB

## Abstract The plant cytotoxin ricin is a heterodimer with a cell surface binding (B) chain and an enzymatically active A chain (RTA) known to act as a specific __N__‐glycosidase. RTA must be separated from B chain to attack rRNA. The X‐ray structure of ricin has been solved recently; here we repo

Structure of ricin B-chain at 2.5 Å reso
Structure of ricin B-chain at 2.5 Å resolution
✍ Earl Rutenber; Jon D. Robertus 📂 Article 📅 1991 🏛 John Wiley and Sons 🌐 English ⚖ 912 KB

## Abstract The heterodimeric plant toxin ricin has been refined to 2.5 Å resolution. The B‐chain lectin (RTB) is described in detail. The protein has two major domains, each of which has a galactose binding site. RTB has no regular secondary structure but displays several Ω loops. Each RTB domain

Structure of ricin A-chain at 2.5 Å
Structure of ricin A-chain at 2.5 Å
✍ Betsy J. Katzin; Edward J. Collins; Jon D. Robertus 📂 Article 📅 1991 🏛 John Wiley and Sons 🌐 English ⚖ 847 KB

## Abstract Ricin has been refined in a crystallographic sense to 2.5 Å resolution and the model for the A‐chain (RTA) is described in detail. Because RTA is the first member of the class of plant toxins to be analyzed, this model probably defines the major structural characteristics of the entire