Hydrolases; Glycosylases; Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds / polysaccharide binding / cellulose catabolic process / hydrolase activity, hydrolyzing O-glycosyl compounds / metal ion binding Similarity search - Function
Monochromator: SI(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength
Wavelength: 0.97685 Å / Relative weight: 1
Reflection
Resolution: 1.75→46.1 Å / Num. obs: 32986 / % possible obs: 99.9 % / Observed criterion σ(I): 2.3 / Redundancy: 4.1 % / Rmerge(I) obs: 0.1 / Net I/σ(I): 10.7
Reflection shell
Resolution: 1.8→1.9 Å / Redundancy: 4.1 % / Rmerge(I) obs: 0.3 / Mean I/σ(I) obs: 4.9 / % possible all: 99.9
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Processing
Software
Name
Version
Classification
REFMAC
5.5.0110
refinement
iMOSFLM
datareduction
SCALA
datascaling
MOLREP
phasing
Refinement
Method to determine structure: MOLECULAR REPLACEMENT Starting model: UNPUBLISHED WILD TYPE CEL6B Resolution: 1.8→20 Å / Cor.coef. Fo:Fc: 0.958 / Cor.coef. Fo:Fc free: 0.938 / SU B: 2.183 / SU ML: 0.07 / Cross valid method: THROUGHOUT / ESU R: 0.133 / ESU R Free: 0.12 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. U VALUES REFINED INDIVIDUALLY.
Rfactor
Num. reflection
% reflection
Selection details
Rfree
0.1911
1672
5.1 %
RANDOM
Rwork
0.15459
-
-
-
obs
0.15644
31289
99.85 %
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Solvent computation
Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK