Endo-b-1,4-xylanase (Xylanase A) D11F/R122D double mutant from Bacillus subtilis Lipari-Szabo order parameters and relaxation data

Effects of Xylanase A double mutation on substrate specificity and structural dynamics.

Endolytically hydrolyzes xylan at a slower rate than WT

5 mm HCN salt-tolerant inverse cold probe with z-axis gradients

D11F/R122D isotropic Lipari-Szabo order parameters

H, N, Ca, and Cb peak assignments for wild type Xylanase A

H, N, Ca, and Cb peak assignments for D11F/R122D double mutant Xylanase A

order parameters and relaxation data for wild type Xylanase A

0.18 mM in 25 mM acetate buffer, pH 5.7, 50 mM NaCl, 10% D2O, 0.03% sodium azide
25 mM acetate buffer, pH 5.7, 50 mM NaCl, 10% D2O, 0.03% sodium azide

R2 values calculated from R1 and R1rho values