Mass: 40.078 Da / Num. of mol.: 9 / Source method: obtained synthetically / Formula: Ca
Sequence details
ENTITY 1 IS A FUSION PROTEIN OF E.COLI MALTOSE BINDING PROTEIN (UNIPROT P0AEX9 (MALE_ECOLI) ...ENTITY 1 IS A FUSION PROTEIN OF E.COLI MALTOSE BINDING PROTEIN (UNIPROT P0AEX9 (MALE_ECOLI) RESIDUES 27-384) TO N-TERMINAL RESIDUES 1-64 OF HUMAN HUNTINGTIN (UNIPROT P42858 (HD_HUMAN)) VIA LINKER AALAAAQTNAAA.
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Experimental details
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Experiment
Experiment
Method: X-RAY DIFFRACTION
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Sample preparation
Crystal
Density Matthews: 3.86 Å3/Da / Density % sol: 68.14 %
Crystal grow
Method: vapor diffusion, hanging drop / pH: 7.2 / Details: pH 7.2, VAPOR DIFFUSION, HANGING DROP
Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength
Wavelength: 0.98 Å / Relative weight: 1
Reflection
Resolution: 3.7→40 Å / Num. obs: 24500 / Redundancy: 1.8 % / Rsym value: 0.02 / Net I/σ(I): 7
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Processing
Software
Name
Version
Classification
HKL-2000
datacollection
PHASES
phasing
REFMAC
5.5.0102
refinement
HKL-2000
datareduction
HKL-2000
datascaling
Refinement
Method to determine structure: SAD / Resolution: 3.7→38.67 Å / Cor.coef. Fo:Fc: 0.907 / Cor.coef. Fo:Fc free: 0.88 / SU B: 92.043 / SU ML: 0.643 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / ESU R Free: 0.747 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
Rfactor
Num. reflection
% reflection
Selection details
Rfree
0.29262
1200
5.4 %
RANDOM
Rwork
0.24491
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obs
0.24754
21188
92.39 %
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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
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