A Caltech Library Service

Crystallographic Analyses of Hyperthermophilic Proteins

Rees, Douglas C. (2001) Crystallographic Analyses of Hyperthermophilic Proteins. In: Hyperthermophilic Enzymes, Part C. Methods in Enzymology. No.334. Academic Press , San Diego, CA, pp. 423-437. ISBN 978-0-12-182235-4.

Full text is not posted in this repository. Consult Related URLs below.

Use this Persistent URL to link to this item:


Following the first structure determination in 1992 of a protein from a hyperthermophilic organism, the rubredoxin from Pyrococcus furiosus, structures of hyperthermophilic proteins have appeared at an ever increasing rate, with more than 50 distinct structures having been submitted to the Protein Data Bank as of October 1999 (Table I). These structure determinations have been undertaken for many of the reasons discussed elsewhere in this volume-to understand the structural basis of thermostability; to more fully characterize proteins with unusual cofactors or active centers; for biotechnological purposes; as homologs of eukaryotic proteins, especially those involved in some aspect of macromolecular biosynthesis; and as part of structural genomics efforts, because they either do, or do not, look like some other proteins. As there is an expectation that hyperthermostable proteins should be more robust and potentially better suited for withstanding the solution conditions and time scales of crystallization experiments, these proteins have provided attractive targets for structural studies. The focus of this chapter is to review the status and some general implications of crystallographic studies on hyperthermophilic proteins, with emphasis on relevant technical aspects of the structure determination, quality of the crystals, and conclusions about thermal stability and other properties of these fascinating proteins.

Item Type:Book Section
Related URLs:
URLURL TypeDescription
Rees, Douglas C.0000-0003-4073-1185
Contact Email
Additional Information:© 2001 by Academic Press. Heated discussions with co-workers and collaborators, particularly M. W. W. Adams and J. B. Howard, are gratefully acknowledged. This work was supported by the Howard Hughes Medical Institute and the National Institutes of Health (GM45162).
Funding AgencyGrant Number
Howard Hughes Medical Institute (HHMI)UNSPECIFIED
Series Name:Methods in Enzymology
Issue or Number:334
Record Number:CaltechAUTHORS:20150108-153028358
Persistent URL:
Official Citation:Douglas C Rees, [32] Crystallographic analyses of hyperthermophilic proteins, In: Michael W. W. Adams, Robert M. Kelly, Editor(s), Methods in Enzymology, Academic Press, 2001, Volume 334, Pages 423-437, ISSN 0076-6879, ISBN 9780121822354, (
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:53400
Deposited By: SWORD User
Deposited On:08 Feb 2015 06:42
Last Modified:10 Nov 2021 20:01

Repository Staff Only: item control page