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Structure paper

TitleIncrease in the thermostability of GH11 xylanase XynJ from Bacillus sp. strain 41M-1 using site saturation mutagenesis.
Journal, issue, pagesEnzyme. Microb. Technol., Vol. 130, Page 109363-109363, Year 2019
Publish dateJul 22, 2019 (structure data deposition date)
AuthorsTakita, T. / Nakatani, K. / Katano, Y. / Suzuki, M. / Kojima, K. / Saka, N. / Mikami, B. / Yatsunami, R. / Nakamura, S. / Yasukawa, K.
External linksEnzyme. Microb. Technol. / PubMed:31421720
MethodsX-ray diffraction
Resolution2.36 - 2.45 Å
Structure data

PDB-6kjl:
Xylanase J from Bacillus sp. strain 41M-1
Method: X-RAY DIFFRACTION / Resolution: 2.45 Å

PDB-6kka:
Xylanase J mutant from Bacillus sp. 41M-1
Method: X-RAY DIFFRACTION / Resolution: 2.36 Å

Chemicals

ChemComp-CA:
Unknown entry

ChemComp-EPE:
4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID / pH buffer*YM

ChemComp-MPD:
(4S)-2-METHYL-2,4-PENTANEDIOL / precipitant*YM

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

ChemComp-CIT:
CITRIC ACID

Source
  • bacillus sp. 41m-1 (bacteria)
KeywordsHYDROLASE / GH11 / xylanase / enzyme

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