Mass: 18.015 Da / Num. of mol.: 1491 / Source method: isolated from a natural source / Formula: H2O
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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: 2.46 Å3/Da / Density % sol: 45.02 %
Crystal grow
Temperature: 289 K / Method: vapor diffusion, sitting drop / pH: 5.5 Details: 0.2 ul of mg/ml protein in 20 mM HEPES pH 7.5, 150 mM NaCl, 10% Glycerol, 0.1% Sodium Azide and 0.5 mM TCEP were mixed with 0.2 ul of the Hampton Index HT #65 (F5) (0.1 M Ammonium acetate, 0. ...Details: 0.2 ul of mg/ml protein in 20 mM HEPES pH 7.5, 150 mM NaCl, 10% Glycerol, 0.1% Sodium Azide and 0.5 mM TCEP were mixed with 0.2 ul of the Hampton Index HT #65 (F5) (0.1 M Ammonium acetate, 0.1 M BIS_TRIS pH 5.5, 17% (w/v) Polyethylene glycol 10,000) and equilibrated against 1.25 M NaCl solution in 96 Well 3 drop Crystallization Plate (Swissci). Before crystallization protein was incubated with 1/50 v/v of 2 mg/ml chymotrypsin solution at 289 K for 3 hours.
Method to determine structure: SAD / Resolution: 1.82→50 Å / Cor.coef. Fo:Fc: 0.967 / Cor.coef. Fo:Fc free: 0.956 / WRfactor Rfree: 0.1795 / WRfactor Rwork: 0.1535 / FOM work R set: 0.8581 / SU B: 5.82 / SU ML: 0.089 / SU R Cruickshank DPI: 0.1231 / SU Rfree: 0.1111 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.123 / ESU R Free: 0.111 Stereochemistry target values: MAXIMUM LIKELIHOOD WITH PHASES Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : WITH TLS ADDED
Rfactor
Num. reflection
% reflection
Selection details
Rfree
0.1926
6926
5 %
RANDOM
Rwork
0.1672
131310
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obs
0.1685
138432
99.16 %
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Solvent computation
Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
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