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Crystal structure of TM1367 from Thermotoga maritima at 1.90 Å resolution reveals an atypical member of the cyclophilin (peptidylprolyl isomerase) fold
Author(s) -
Jin Kevin Kai,
Krishna S. Sri,
Schwarzenbacher Robert,
McMullan Daniel,
Abdubek Polat,
Agarwalla Sanjay,
Ambing Eileen,
Axelrod Herbert,
Canaves Jaume M.,
Chiu HsiuJu,
Deacon Ashley M.,
DiDonato Michael,
Elsliger MarcAndré,
Feuerhelm Julie,
Godzik Adam,
Grittini Carina,
Grzechnik Slawomir K.,
Hale Joanna,
Hampton Eric,
Haugen Justin,
Hornsby Michael,
Jaroszewski Lukasz,
Klock Heath E.,
Knuth Mark W.,
Koesema Eric,
Kreusch Andreas,
Kuhn Peter,
Lesley Scott A.,
Miller Mitchell D.,
Moy Kin,
Nigoghossian Edward,
Okach Linda,
Oommachen Silvya,
Paulsen Jessica,
Quijano Kevin,
Reyes Ron,
Rife Chris,
Stevens Raymond C.,
Spraggon Glen,
van den Bedem Henry,
Velasquez Jeff,
White Aprilfawn,
Wolf Guenter,
Han Gye Won,
Xu Qingping,
Hodgson Keith O.,
Wooley John,
Wilson Ian A.
Publication year - 2006
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.20894
Subject(s) - structural genomics , thermotoga maritima , periplasmic space , peptidylprolyl isomerase , crystallography , isomerase , molecular replacement , chemistry , protein structure , crystal structure , computational biology , biology , biochemistry , gene , escherichia coli