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The Mycobacterium smegmatis Gre-factor homologue MSMEG_6292 is an RNA polymerase secondary channel-binding protein. To understand its structure and function, it was cloned, expressed, purified and crystallized, and crystallographic diffraction data were collected for both the native protein and a platinum derivative.

The structure of T. aurantiacus xylanase solved to small-molecule accuracy at atomic resolution (1.11 Å) at 293 K and at ultrahigh resolution (0.89 Å) at 100 K provides insights into the plasticity of salt bridges, the temperature-dependent deformation and the water structure of the enzyme, which belongs to the ubiquitous TIM-barrel fold.
