Data of serial synchrotron crystallography of xylanase GH11 from Thermoanaerobacterium saccharolyticum.

ABSTRACT: The endo-1,4-β-xylanase GH11 from the hemicellulose-degrading bacterium Thermoanaerobacterium saccharolyticum (TsaGH11) has been characterized as a thermophilic enzyme. TsaGH11 exhibits its maximum activity at pH 5.0 and 70 °C, along with superior properties towards beechwood xylan, with a K_m of 12.9 mg mL⁻¹ and a K_cat of 34,015.3 s⁻¹. The room-temperature and cryogenic crystal structures of TsaGH11 were determined using serial synchrotron crystallography (SSX) and conventional macromolecular crystallography techniques, respectively. The high-resolution crystal structure of TsaGH11 was successfully determined, and the flexibility of the thumb domain at room temperature was elucidated. During SSX data collection, a high density of crystal samples in the sample h

SUBMITTER: Nam KH 

PROVIDER: S-EPMC10828573 | biostudies-literature | 2024 Feb

REPOSITORIES: biostudies-literature