Mass: 18.015 Da / Num. of mol.: 750 / Source method: isolated from a natural source / Formula: H2O
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Details
Compound details
ENGINEERED MUTATION IN CHAIN A, SER 954 TO ALA ENGINEERED MUTATION IN CHAIN B, SER 954 TO ALA ...ENGINEERED MUTATION IN CHAIN A, SER 954 TO ALA ENGINEERED MUTATION IN CHAIN B, SER 954 TO ALA CATALYTIC ACTIVITY: ENDOHYDROLYSIS OF 1,4-BETA-D-XYLOSIDIC LINKAGES IN XYLANS.
Sequence details
ONLY THE FERULOYL ESTERASE DOMAIN WAS SUBCLONED. S954A MUTANT. THE SEQUENCE CONFLICTS (RESIDUES ...ONLY THE FERULOYL ESTERASE DOMAIN WAS SUBCLONED. S954A MUTANT. THE SEQUENCE CONFLICTS (RESIDUES 1017 AND 1018) ARE DUE TO ERRORS IN THE UNIPROT ENTRY FROM THE ORIGINAL SEQUENCING OF THE PROTEIN.
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Experimental details
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Experiment
Experiment
Method: X-RAY DIFFRACTION / Number of used crystals: 1
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Sample preparation
Crystal
Density Matthews: 2.95 Å3/Da / Density % sol: 58 %
Crystal grow
pH: 7.5 Details: NA ACETATE 1M CD ACETATE 50 MM GLYCEROL 5% HEPES PH 7.5 100 MM
Resolution: 1.4→79.06 Å / Cor.coef. Fo:Fc: 0.981 / Cor.coef. Fo:Fc free: 0.974 / SU B: 0.477 / SU ML: 0.019 / Cross valid method: THROUGHOUT / ESU R: 0.039 / ESU R Free: 0.038 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
Rfactor
Num. reflection
% reflection
Selection details
Rfree
0.134
7700
5 %
RANDOM
Rwork
0.111
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obs
0.113
146352
97.8 %
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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: BABINET MODEL WITH MASK