Journal article

Crystal structure of a novel Thermotoga maritima enzyme (TM1112) from the cupin family at 1.83 A resolution.

Publication status:: Published

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APA Style

McMullan, D., Schwarzenbacher, R., Jaroszewski, L., von Delft, F., Klock, H., Vincent, J., Quijano, K., Abdubek, P., Ambing, E., Biorac, T., Brinen, L., Canaves, J., Dai, X., Deacon, A., DiDonato, M., Elsliger, M., Eshaghi, S., Floyd, R., Godzik, A., … Kreusch, A. (2004). Crystal structure of a novel Thermotoga maritima enzyme (TM1112) from the cupin family at 1.83 A resolution. Proteins, 56(3), 615–618.

MLA Style

McMullan, D., et al. “Crystal Structure of a Novel Thermotoga Maritima Enzyme (TM1112) from the Cupin Family at 1.83 A Resolution.” Proteins, vol. 56, no. 3, 2004, pp. 615–18.

Chicago Style

McMullan, D, R Schwarzenbacher, L Jaroszewski, F von Delft, H Klock, J Vincent, K Quijano, et al. 2004. “Crystal Structure of a Novel Thermotoga Maritima Enzyme (TM1112) from the Cupin Family at 1.83 A Resolution.” Proteins 56 (3): 615–18.
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Publisher copy:: 10.1002/prot.20139

Authors

+ McMullan, D More by this author

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Author

+ Schwarzenbacher, R More by this author

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Author

+ Jaroszewski, L More by this author

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Author

+ von Delft, F More by this author

Institution:

University of Oxford

Division:

MSD

Department:

NDM

Sub department:

Structural Genomics Consortium

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Author

+ Klock, H More by this author

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Bibliographic Details

Journal:: Proteins More from this journal
Volume:: 56
Issue:: 3
Pages:: 615-618
Publication date:: 2004-08-01
DOI:: 10.1002/prot.20139
EISSN:: 1097-0134
ISSN:: 0887-3585

Item Description

Language:: English
Keywords:: Amino Acid Sequence

Magnetic Resonance Spectroscopy

Thermotoga maritima

Protein Structure, Secondary

Structural Homology, Protein

Models, Molecular

Conserved Sequence

Molecular Sequence Data

Binding Sites

Crystallization

Bacterial Proteins
Pubs id:: pubs:32766
UUID:: uuid:33990276-61a4-464a-a3c1-8d90dbd00bab
Local pid:: pubs:32766
Source identifiers:: 32766
Deposit date:: 2012-12-19

Terms of use

Copyright date:: 2004

Licence:: Terms and Conditions of Use for Oxford University Research Archive

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