Mass: 62649.336 Da / Num. of mol.: 2 / Fragment: HEPHA4 ECTODOMAIN, RESIDUES 20-547 Source method: isolated from a genetically manipulated source Source: (gene. exp.) HOMO SAPIENS (human) / Plasmid: PHLSEC / Cell line (production host): HEK293T / Production host: HOMO SAPIENS (human) References: UniProt: P54764, receptor protein-tyrosine kinase
Sequence details
SEQUENCE CORRESPONDS TO HEPHA4 RESIDUES 27-547 FUSED TO AN N-TERMINAL SECRETION SIGNAL SEQUENCE AND ...SEQUENCE CORRESPONDS TO HEPHA4 RESIDUES 27-547 FUSED TO AN N-TERMINAL SECRETION SIGNAL SEQUENCE AND A POLY-HISTIDINE TAG
-
Experimental details
-
Experiment
Experiment
Method: X-RAY DIFFRACTION
-
Sample preparation
Crystal
Density Matthews: 6.16 Å3/Da / Density % sol: 76.7 % Description: WE USED THE NEW CC CUTOFF CRITERIA FOR DETERMINING THE HIGH RES CUTOFF. CC-HALF IN THE HIGH RES SHELL IS 17.7
Crystal grow
Details: 1.8 M AMMONIUM PHOSPHATE, 100 MM HEPES PH 7.4, ADDITIVE = EPHRINB2 IN A 1:1 MOLAR RATIO. WE SAW NO SIGN OF EPHRINB2 IN THE CRYSTAL STRUCTURE. THE USUAL BINDING SITE ON HEPHA4 WAS OCCUPIED BY ...Details: 1.8 M AMMONIUM PHOSPHATE, 100 MM HEPES PH 7.4, ADDITIVE = EPHRINB2 IN A 1:1 MOLAR RATIO. WE SAW NO SIGN OF EPHRINB2 IN THE CRYSTAL STRUCTURE. THE USUAL BINDING SITE ON HEPHA4 WAS OCCUPIED BY AN EPHA4-EPHA4 CRYSTAL CONTACT.
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Data collection
Diffraction
ID
Mean temperature (K)
Crystal-ID
1
100
1
2
100
1
Diffraction source
Source
Site
Beamline
ID
Wavelength
SYNCHROTRON
Diamond
I24
1
0.9173
SYNCHROTRON
Diamond
I04
2
0.9173
Radiation
ID
Protocol
Monochromatic (M) / Laue (L)
Scattering type
Wavelength-ID
1
SINGLEWAVELENGTH
M
x-ray
1
2
SINGLEWAVELENGTH
M
x-ray
1
Radiation wavelength
Wavelength: 0.9173 Å / Relative weight: 1
Reflection
Resolution: 3.65→83 Å / Num. obs: 34863 / % possible obs: 99.9 % / Observed criterion σ(I): 0 / Redundancy: 20 % / Biso Wilson estimate: 144.4 Å2 / Rmerge(I) obs: 0.19 / Net I/σ(I): 14.7
Reflection shell
Resolution: 3.65→3.7 Å / Redundancy: 20 % / Mean I/σ(I) obs: 0.48 / % possible all: 100
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