Mass: 41819.730 Da / Num. of mol.: 1 Fragment: Juxtamembrane segment and kinase domain: residues 577-947 Mutation: Y608A Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: EPHA3, ETK, ETK1, HEK, TYRO4 / Plasmid: pET28a-LIC / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) References: UniProt: P29320, receptor protein-tyrosine kinase
#2: Protein/peptide
peptidesubstrate
Mass: 1525.532 Da / Num. of mol.: 1 / Source method: obtained synthetically Details: Peptide synthesized with phosphorylation at the +2 tyrosine position
Type: RIGAKU RAXIS IV / Detector: IMAGE PLATE / Date: Feb 6, 2007
Radiation
Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength
Wavelength: 1.54178 Å / Relative weight: 1
Reflection
Redundancy: 3.4 % / Av σ(I) over netI: 28.36 / Number: 113957 / Rmerge(I) obs: 0.044 / Χ2: 1.43 / D res high: 1.7 Å / D res low: 30 Å / Num. obs: 33335 / % possible obs: 98.3
Diffraction reflection shell
Highest resolution (Å)
Lowest resolution (Å)
% possible obs (%)
ID
Rmerge(I) obs
Chi squared
Redundancy
3.66
30
99.9
1
0.032
1.066
3.6
2.91
3.66
99.8
1
0.036
1.21
3.6
2.54
2.91
99.9
1
0.045
1.143
3.6
2.31
2.54
100
1
0.055
1.64
3.6
2.14
2.31
100
1
0.069
1.662
3.5
2.02
2.14
99.9
1
0.09
1.769
3.5
1.91
2.02
99.9
1
0.131
1.628
3.5
1.83
1.91
100
1
0.184
1.485
3.5
1.76
1.83
99.5
1
0.256
1.355
3.3
1.7
1.76
84.1
1
0.312
1.257
2.4
Reflection
Resolution: 1.7→30 Å / Num. obs: 33335 / % possible obs: 98.3 % / Redundancy: 3.4 % / Rmerge(I) obs: 0.044 / Χ2: 1.427 / Net I/σ(I): 28.359
Reflection shell
Resolution (Å)
Redundancy (%)
Rmerge(I) obs
Num. unique all
Χ2
Diffraction-ID
% possible all
1.7-1.76
2.4
0.312
2839
1.257
1
84.1
1.76-1.83
3.3
0.256
3367
1.355
1
99.5
1.83-1.91
3.5
0.184
3349
1.485
1
100
1.91-2.02
3.5
0.131
3339
1.628
1
99.9
2.02-2.14
3.5
0.09
3404
1.769
1
99.9
2.14-2.31
3.5
0.069
3334
1.662
1
100
2.31-2.54
3.6
0.055
3406
1.64
1
100
2.54-2.91
3.6
0.045
3370
1.143
1
99.9
2.91-3.66
3.6
0.036
3419
1.21
1
99.8
3.66-30
3.6
0.032
3508
1.066
1
99.9
-
Phasing
Phasing
Method: molecular replacement
Phasing MR
Rfactor: 34.22 / Model details: Phaser MODE: MR_AUTO
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