1JEW

CRYO-EM STRUCTURE OF COXSACKIEVIRUS B3(M STRAIN) WITH ITS CELLULAR RECEPTOR, COXSACKIEVIRUS AND ADENOVIRUS RECEPTOR (CAR).

ELECTRON MICROSCOPY

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1	ELECTRON MICROSCOPY RECONSTRUCTION	7.5	298	WARNING: THIS IS AN CRYO-ELECTRON MICROSCOPY MODEL DEPOSITION. CRYO-EM INFORMATION HAS BEEN INCLUDED IN THE PDB FILE., pH 7.5, ELECTRON MICROSCOPY RECONSTRUCTION, temperature 298K

Sample
COXSACKIEVIRUS B3(M STRAIN) WITH ITS CELLULAR RECEPTOR

Specimen Preparation
Sample Aggregation State	PARTICLE
Vitrification Instrument
Cryogen Name
Sample Vitrification Details	CVB3 WAS INCUBATED WITH CAR SAMPLE FOR 1 HOURS AT 25 DEGREES CELSIUS (298 KELVIN) USING A FOUR-FOLD EXCESS OF CAR FOR EACH OF THE SIXTY POSSIBLE BINDI ...	CVB3 WAS INCUBATED WITH CAR SAMPLE FOR 1 HOURS AT 25 DEGREES CELSIUS (298 KELVIN) USING A FOUR-FOLD EXCESS OF CAR FOR EACH OF THE SIXTY POSSIBLE BINDING SITES PER VIRION. AFTER INCUBATION, SAMPLES WERE PREPARED AS THIN LAYERS OF VITREOUS ICE AND MAINTAINED AT NEAR LIQUID NITROGEN TEMPERATURE IN THE ELECTRON MICROSCOPE WITH A GATAN 626 CRYOTRANSFER HOLDER.

3D Reconstruction
Reconstruction Method	SINGLE PARTICLE
Number of Particles	635
Reported Resolution (Å)	22
Resolution Method	OTHER
Other Details	THE RESOLUTION OF THE FINAL RECONSTRUCTED DENSITY WAS DETERMINED TO BE AT LEAST 22 ANGSTROMS, AS MEASURED BY RANDOMLY SPLITTING THE PARTICLES INTO ...	THE RESOLUTION OF THE FINAL RECONSTRUCTED DENSITY WAS DETERMINED TO BE AT LEAST 22 ANGSTROMS, AS MEASURED BY RANDOMLY SPLITTING THE PARTICLES INTO TWO SETS AND COMPARING STRUCTURE FACTORS OBTAINED FROM SEPARATE RECONSTRUCTIONS (BAKER ET AL. 1991, BIOPHYS.J. 60, 1445-1456). THE EIGENVALUE SPECTRUM GAVE AN INDICATION OF THE RANDOMNESS OF THE DATA THAT WAS INCLUDED IN THE RECONSTRUCTION. THE COMPLETENESS OF THE DATA WAS VERIFIED IN THAT ALL EIGENVALUES EXCEEDED 1.0.
Refinement Type
Symmetry Type	POINT
Point Symmetry	I

Map-Model Fitting and Refinement
Id	1
Refinement Space	REAL
Refinement Protocol	OTHER
Refinement Target
Overall B Value
Fitting Procedure
Details	METHOD--Acta Cryst. D56, 1341 REFINEMENT PROTOCOL--EMFIT DETAILS--THE DIFFERENCE MAP BETWEEN CVB3-CAR COMPLEX AND NATIVE CVB WAS CALCULATED AND THEN ...	METHOD--Acta Cryst. D56, 1341 REFINEMENT PROTOCOL--EMFIT DETAILS--THE DIFFERENCE MAP BETWEEN CVB3-CAR COMPLEX AND NATIVE CVB WAS CALCULATED AND THEN FITTED WITH THE N-TERMINAL DOMAIN OF CAR (1KAC, B-CHAIN). THE AUTOMATIC FITTING WAS DONE USI PROGRAM EMFIT DESCRIBED IN ACTA CRYST. D56, 1341-1349. THE CRYSTAL STRUCTURE OF POLIOVIRUS WAS PLACED INTO THE

Data Acquisition
Detector Type	KODAK SO-163 FILM
Electron Dose (electrons/Å**2)	20

Imaging Experiment	1
Date of Experiment	2000-06-01
Temperature (Kelvin)	120
Microscope Model	FEI/PHILIPS CM300FEG/T
Minimum Defocus (nm)	1500
Maximum Defocus (nm)	4600
Minimum Tilt Angle (degrees)
Maximum Tilt Angle (degrees)
Nominal CS
Imaging Mode	BRIGHT FIELD
Specimen Holder Model
Nominal Magnification	61000
Calibrated Magnification
Source	FIELD EMISSION GUN
Acceleration Voltage (kV)	300
Imaging Details

EM Software
Task	Software Package	Version
RECONSTRUCTION	PURDUE PROGRAMS

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM133198.