Mass: 20528.113 Da / Num. of mol.: 1 / Fragment: RESIDUES 27-198 Source method: isolated from a genetically manipulated source Details: PROTEIN-HEME CROSS-LINK FROM NZ OF LYS 70 TO CHA OF HEC 200. PROTEIN-HEME CROSSLINK FROM SG OF CYS 136 TO CAB OF HEC 200. PROTEIN-HEME CROSSLINK FROM SG OF CYS 139 TO CAC OF HEC 200 Source: (gene. exp.) NITROSOMONAS EUROPAEA (bacteria) Description: CONTAINS ADDITIONAL N-TERMINAL METHIONINE AND AT THE TERMINUS THE ADDITIONS RESIDUES KLAAALEHHHHHH Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: Q50927
Mass: 18.015 Da / Num. of mol.: 138 / Source method: isolated from a natural source / Formula: H2O
Sequence details
RECOMBINANT PROTEIN CONTAINS ADDITIONAL N-TERMINAL METHIONINE AND C-TERMINAL TAG KLAAALEHHHHHH
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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: 2.59 Å3/Da / Density % sol: 52.08 % Description: THE STRUCTURE WAS SOLVED BY SAD USING A DATASET COLLECTED AT CR K-ALPHA. PHASED USING SHELX AND SHARP. THE INITIAL MODEL WAS THEN USED TO PHASE THE HIGHER RESOLUTION CU K-ALPHA DATASET
Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength
Wavelength: 1.5418 Å / Relative weight: 1
Reflection
Resolution: 1.69→43 Å / Num. obs: 17344 / % possible obs: 80.1 % / Observed criterion σ(I): 2 / Redundancy: 3.4 % / Biso Wilson estimate: 24.2 Å2 / Rmerge(I) obs: 0.04 / Net I/σ(I): 19.1
Reflection shell
Resolution: 1.69→1.75 Å / Redundancy: 1.1 % / Rmerge(I) obs: 0.1 / Mean I/σ(I) obs: 2.8 / % possible all: 15
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Processing
Software
Name
Version
Classification
REFMAC
5.2.0019
refinement
HKL-2000
datareduction
SCALEPACK
datascaling
Refinement
Method to determine structure: MOLECULAR REPLACEMENT Starting model: INITIAL MODEL FROM SULPHUR SAD STRUCTURE Resolution: 1.8→43.35 Å / Cor.coef. Fo:Fc: 0.953 / Cor.coef. Fo:Fc free: 0.937 / SU ML: 0.072 / Cross valid method: THROUGHOUT / ESU R: 0.13 / ESU R Free: 0.126 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. RESIDUES 31-40 AND 82-85 ARE NOT VISIBLE IN THE ELECTRON DENSITY
Rfactor
Num. reflection
% reflection
Selection details
Rfree
0.231
921
5 %
RANDOM
Rwork
0.195
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obs
0.197
17341
91 %
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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