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1DUG

STRUCTURE OF THE FIBRINOGEN G CHAIN INTEGRIN BINDING AND FACTOR XIIIA CROSSLINKING SITES OBTAINED THROUGH CARRIER PROTEIN DRIVEN CRYSTALLIZATION

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsNSLS BEAMLINE X4A
Synchrotron siteNSLS
BeamlineX4A
Temperature [K]100
Detector technologyIMAGE PLATE
Collection date1997-03-15
DetectorFUJI
Spacegroup nameP 41 21 2
Unit cell lengths105.780, 105.780, 137.230
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution28.000 - 1.800
R-factor0.185
Rwork0.185
R-free0.22600
RMSD bond length0.007
RMSD bond angle1.425
Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwareAMoRE
Refinement softwareX-PLOR (3.851)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]28.0002.000
High resolution limit [Å]1.7001.800
Rmerge0.0540.250
Total number of observations376772

*

Number of reflections67736
Completeness [%]89.266.1
Redundancy5.563.1
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP4.6-170

*

PEG 3350, sodium acetate, sodium chloride, ammonium sulfate, Tris, reduced glutathione, pH 4.6, VAPOR DIFFUSION, HANGING DROP
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropprotein10 (mg/ml)
101reservoirammonium sulfate35 (mM)
21dropPEG33508 (%)
31dropsodium acetate50 (mM)
41dropsodium chloride25 (mM)
51dropammonium sulfate17.5 (mM)
61dropTris-HCl5 (mM)
71dropglutathinoe5 (mM)
81reservoirPEG335016 (%)
91reservoirsodium acetate100 (mM)

218853

건을2024-04-24부터공개중

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