Mass: 18.015 Da / Num. of mol.: 238 / 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: 3.6 Å3/Da / Density % sol: 65.9 % / Description: NONE
Crystal grow
pH: 8.5 Details: CRYSTALLIZATION SOLUTION: 100MM TRIS-HCL PH8.5, 2M AMMONIUM SULFATE. THE DROP WAS MADE BY ADDING 1UL OF PROTEIN PLUS 1.8UL OF CRYSTALLIZATION SOLUTION AND 0.2UL OF 2MM SIROHYDROCHLORIN AND 0. ...Details: CRYSTALLIZATION SOLUTION: 100MM TRIS-HCL PH8.5, 2M AMMONIUM SULFATE. THE DROP WAS MADE BY ADDING 1UL OF PROTEIN PLUS 1.8UL OF CRYSTALLIZATION SOLUTION AND 0.2UL OF 2MM SIROHYDROCHLORIN AND 0.2UL OF COBALT CHLORIDE IN AEROBIC CONDITIONS.
Resolution: 1.7→85.44 Å / Cor.coef. Fo:Fc: 0.966 / Cor.coef. Fo:Fc free: 0.962 / SU B: 1.518 / SU ML: 0.05 / Cross valid method: THROUGHOUT / ESU R: 0.079 / ESU R Free: 0.076 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. THE SIDE-CHAINS OF THE AMINO ACID RESIDUES- GLU22, GLU23, LYS51, MET52, GLU93, LYS110, ARG218 WERE MODELLED WITH 0.5 OF OCCUPANCY DUE TO ...Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. THE SIDE-CHAINS OF THE AMINO ACID RESIDUES- GLU22, GLU23, LYS51, MET52, GLU93, LYS110, ARG218 WERE MODELLED WITH 0.5 OF OCCUPANCY DUE TO THE LACK OF ELECTRON DENSITY PROBABLY DUE TO DISORDER. THE FOLLOWING AMINO ACID RESIDUES WERE MODELLED WITH DOUBLE CONFORMATION- MET31, ARG34, GLU133, ARG173, VAL198, LEU206, LEU209, ASP227, ARG236.
Rfactor
Num. reflection
% reflection
Selection details
Rfree
0.18779
2379
5.1 %
RANDOM
Rwork
0.17215
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obs
0.17296
44493
96.79 %
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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