Journal: J.Biol.Chem. / Year: 2006 Title: Structure of the Escherichia Coli O157:H7 Heme Oxygenase Chus in Complex with Heme and Enzymatic Inactivation by Mutation of the Heme Coordinating Residue His-193. Authors: Suits, M.D. / Jaffer, N. / Jia, Z.
Mass: 18.015 Da / Num. of mol.: 391 / Source method: isolated from a natural source / Formula: H2O
Nonpolymer details
1,2-ETHANEDIOL (EDO): EDO WAS AN ADDITIVE IN CRYSTALLIZATION. PROTOPORPHYRIN IX CONTAINING FE (HEM): ...1,2-ETHANEDIOL (EDO): EDO WAS AN ADDITIVE IN CRYSTALLIZATION. PROTOPORPHYRIN IX CONTAINING FE (HEM): CO-PURIFIED WITH PROTEIN FORMIC ACID (FMT): FMT WAS AN ADDITIVE IN CRYSTALLIZATION.
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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: 49.93 % / Description: NONE
Crystal grow
Temperature: 277 K / Method: vapor diffusion, sitting drop / pH: 8 Details: 20MG/ML PROTEIN, 12-15% PEG 0.15-0.2M MAGNESIUM FORMATE, AND 10-20MM NAD, PH 8.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K
Resolution: 1.45→30.08 Å / Cor.coef. Fo:Fc: 0.977 / Cor.coef. Fo:Fc free: 0.968 / SU B: 2.049 / SU ML: 0.035 / Cross valid method: THROUGHOUT / ESU R: 0.059 / ESU R Free: 0.057 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. U VALUES WITH TLS ADDED. RESIDUES 170-175 DISORDERED, NOT MODELED. ELECTRON DENSITY AROUND PRO15 AND GLY16 SUGGESTS FLEXIBILITY.
Rfactor
Num. reflection
% reflection
Selection details
Rfree
0.17253
3371
5 %
RANDOM
Rwork
0.13259
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obs
0.13462
63391
98.69 %
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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