Journal article

Crystal structure of a formiminotetrahydrofolate cyclodeaminase (TM1560) from Thermotoga maritima at 2.80 A resolution reveals a new fold.

Publication status:: Published

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APA Style

Xu, Q., Schwarzenbacher, R., McMullan, D., Abdubek, P., Ambing, E., Biorac, T., Canaves, J., Chiu, H., Dai, X., Deacon, A., DiDonato, M., Elsliger, M., Godzik, A., Grittini, C., Grzechnik, S., Hampton, E., Hornsby, M., Jaroszewski, L., Klock, H., … Miller, M. D. (2005). Crystal structure of a formiminotetrahydrofolate cyclodeaminase (TM1560) from Thermotoga maritima at 2.80 A resolution reveals a new fold. Proteins, 58(4), 976–981.

MLA Style

Xu, Q., et al. “Crystal Structure of a Formiminotetrahydrofolate Cyclodeaminase (TM1560) from Thermotoga Maritima at 2.80 A Resolution Reveals a New Fold.” Proteins, vol. 58, no. 4, 2005, pp. 976–81.

Chicago Style

Xu, Q, R Schwarzenbacher, D McMullan, P Abdubek, E Ambing, T Biorac, J Canaves, et al. 2005. “Crystal Structure of a Formiminotetrahydrofolate Cyclodeaminase (TM1560) from Thermotoga Maritima at 2.80 A Resolution Reveals a New Fold.” Proteins 58 (4): 976–81.
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Publisher copy:: 10.1002/prot.20364

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+ Xu, Q More by this author

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+ Schwarzenbacher, R More by this author

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+ McMullan, D More by this author

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+ Abdubek, P More by this author

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+ Ambing, E More by this author

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Bibliographic Details

Journal:: Proteins More from this journal
Volume:: 58
Issue:: 4
Pages:: 976-981
Publication date:: 2005-03-01
DOI:: 10.1002/prot.20364
EISSN:: 1097-0134
ISSN:: 0887-3585

Item Description

Language:: English
Keywords:: Amino Acid Sequence

Crystallography, X-Ray

Enzyme Stability

Protein Structure, Secondary

Binding Sites

Molecular Sequence Data

Protein Conformation

Thermotoga maritima

Molecular Conformation

Models, Chemical

Ammonia-Lyases

Protein Structure, Tertiary

Crystallization

Models, Molecular
Pubs id:: pubs:32955
UUID:: uuid:33267608-469d-4163-9c5f-8bf1fe1fdf4d
Local pid:: pubs:32955
Source identifiers:: 32955
Deposit date:: 2012-12-19

Terms of use

Copyright date:: 2005

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

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