Mass: 18.015 Da / Num. of mol.: 159 / Source method: isolated from a natural source / Formula: H2O
Sequence details
THIS PROTEIN INCLUDES ONLY THE COILED-COIL DOMAIN OF GIT1 AND AS A CLONING ARTIFACT, THE PROTEIN ...THIS PROTEIN INCLUDES ONLY THE COILED-COIL DOMAIN OF GIT1 AND AS A CLONING ARTIFACT, THE PROTEIN SEQUENCE CONTAINS THE N-TERMINAL RESIDUES GPLGS.
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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 Å3/Da / Density % sol: 36.9 % Description: STRUCTURE WAS SOLVED BY SAD USING AN ISOMORPHOUS CRYSTAL DIFFRACTING TO LOWER RESOLUTION.
Monochromator: SI(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength
Wavelength: 0.9699 Å / Relative weight: 1
Reflection
Resolution: 1.4→20 Å / Num. obs: 22529 / % possible obs: 99.6 % / Observed criterion σ(I): 5 / Redundancy: 7 % / Rmerge(I) obs: 0.07 / Net I/σ(I): 23.5
Reflection shell
Resolution: 1.4→1.46 Å / Redundancy: 5.7 % / Rmerge(I) obs: 0.2 / Mean I/σ(I) obs: 7.8 / % possible all: 97.1
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Processing
Software
Name
Version
Classification
REFMAC
5.2.0019
refinement
DENZO
datareduction
SCALEPACK
datascaling
PHENIX
phasing
Refinement
Method to determine structure: SAD Starting model: NONE Resolution: 1.4→19.4 Å / Cor.coef. Fo:Fc: 0.963 / Cor.coef. Fo:Fc free: 0.949 / SU B: 1.901 / SU ML: 0.036 / Cross valid method: THROUGHOUT / ESU R: 0.077 / ESU R Free: 0.067 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
Rfactor
Num. reflection
% reflection
Selection details
Rfree
0.199
1149
5.1 %
RANDOM
Rwork
0.161
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obs
0.163
21360
99.6 %
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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: BABINET MODEL WITH MASK