Crystallizability of an engineered monomeric mutant of FK506-binding protein from Shewanella sp. SIB1: preliminary diffraction data analysis
Background and Objective: A 22 kDa FK506-binding protein from a psychrophilic bacterium Shewanella sp. SIB1 (SIB1 FKBP22) is a member of peptidyl prolyl cis-trans isomerase (PPIase). This protein is homodimer with a V-shaped form, consisting of N and C-domains, that are connected through a long α-he...
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Format: | Article |
Language: | English English |
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ANSInet
2016
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Online Access: | https://eprints.ums.edu.my/id/eprint/19164/1/Crystallizability%20of%20an%20engineered%20monomeric%20mutant%20of%20FK506.pdf https://eprints.ums.edu.my/id/eprint/19164/7/Crystallizability%20of%20an%20Engineered%20Monomeric%20Mutant%20of.pdf https://eprints.ums.edu.my/id/eprint/19164/ http://dx.doi.org/10.3923/jbs.2016.141.147 |
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https://eprints.ums.edu.my/id/eprint/19164/1/Crystallizability%20of%20an%20engineered%20monomeric%20mutant%20of%20FK506.pdfhttps://eprints.ums.edu.my/id/eprint/19164/7/Crystallizability%20of%20an%20Engineered%20Monomeric%20Mutant%20of.pdf
https://eprints.ums.edu.my/id/eprint/19164/
http://dx.doi.org/10.3923/jbs.2016.141.147