carbon-oxygen lyase activity, acting on polysaccharides / pectin catabolic process / periplasmic space / metal ion binding Similarity search - Function
Mass: 18.015 Da / Num. of mol.: 498 / Source method: isolated from a natural source / Formula: H2O
-
Details
Sequence details
N-TERMINAL HISTIDINE AFFINITY TAG AND RESIDUES 18-556 ONLY.
-
Experimental details
-
Experiment
Experiment
Method: X-RAY DIFFRACTION / Number of used crystals: 1
-
Sample preparation
Crystal
Density Matthews: 3.2 Å3/Da / Density % sol: 61.6 % / Description: NONE
Crystal grow
Temperature: 292 K / Method: vapor diffusion, hanging drop / pH: 7 Details: CRYSTALS OF VVPL2 DEVELOPED VIA HANGING DROP VAPOUR DIFFUSION METHOD AT A PROTEIN CONCENTRATION OF 15 MG/ML BY MIXING EQUAL AMOUNTS OF THE PROTEIN SOLUTION WITH A MOTHER LIQUOR CONSISTING OF ...Details: CRYSTALS OF VVPL2 DEVELOPED VIA HANGING DROP VAPOUR DIFFUSION METHOD AT A PROTEIN CONCENTRATION OF 15 MG/ML BY MIXING EQUAL AMOUNTS OF THE PROTEIN SOLUTION WITH A MOTHER LIQUOR CONSISTING OF 16% (W/V) POLYETHYLENE GLYCOL 3,350, 0.14 M NA/K TARTRATE, AND 0.1 M HEPES (PH 7.0) AT 19 DEGREES CELSIUS. CRYSTALS WERE CRYOPROTECTED BY BRIEF CRYSTAL IMMERSION INTO A SOLUTION OF THE RESERVOIR SOLUTION SUPPLEMENTED WITH 25% ETHYLENE GLYCOL, AND SUBSEQUENTLY FROZEN IN A LIQUID NITROGEN STREAM PRIOR TO DIFFRACTION EXPERIMENTS.
Resolution: 1.9→122.2 Å / Cor.coef. Fo:Fc: 0.97 / Cor.coef. Fo:Fc free: 0.951 / SU B: 2.439 / SU ML: 0.072 / Cross valid method: THROUGHOUT / ESU R: 0.107 / ESU R Free: 0.111 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. U VALUES REFINED INDIVIDUALLY. RESIDUES 0-17 THAT INCLUDE THE HISTIDINE-AFFINITY TAG, INTERDIGITATE FROM AN ADJACENT PROTEIN MOLECULE
Rfactor
Num. reflection
% reflection
Selection details
Rfree
0.19678
3266
5.1 %
RANDOM
Rwork
0.15585
-
-
-
obs
0.1579
61132
99.59 %
-
Solvent computation
Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK