Journal: J.Mol.Catal., B Enzym. / Year: 2014 Title: Structure of the Nadh-Dependent Thermostable Alcohol Dehydrogenase Tadh from Thermus Sp. Atn1 Provides a Platform for Engineering Specificity and Improved Compatibility with Inorganic Cofactor- ...Title: Structure of the Nadh-Dependent Thermostable Alcohol Dehydrogenase Tadh from Thermus Sp. Atn1 Provides a Platform for Engineering Specificity and Improved Compatibility with Inorganic Cofactor-Regeneration Catalysts Authors: Man, H. / Gargulio, S. / Frank, A. / Hollmann, F. / Grogan, G.
Resolution: 2.74→112.52 Å / Cor.coef. Fo:Fc: 0.948 / Cor.coef. Fo:Fc free: 0.914 / SU B: 14.236 / SU ML: 0.28 / Cross valid method: THROUGHOUT / ESU R Free: 0.36 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
Rfactor
Num. reflection
% reflection
Selection details
Rfree
0.24758
2045
5 %
RANDOM
Rwork
0.19157
-
-
-
obs
0.19431
38461
99.96 %
-
Solvent computation
Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK