4V8W

Structure and conformational variability of the Mycobacterium tuberculosis fatty acid synthase multienzyme complex


ELECTRON MICROSCOPY
Sample
Mycobacterium tuberculosis fatty acid synthase multienzyme complex
Specimen Preparation
Sample Aggregation StatePARTICLE
Vitrification InstrumentFEI VITROBOT MARK III
Cryogen NameETHANE
Sample Vitrification Details
3D Reconstruction
Reconstruction MethodSINGLE PARTICLE
Number of Particles9136
Reported Resolution (Å)17.5
Resolution Method
Other DetailsTHE MODEL IS DERIVED FROM PDB ENTRY 3ZEN BOEHRINGER ET AL., 2013 AND REPRESENTS A RIGID BODY DOCKING OF THE MODEL INTO A CRYO-EM MAP. IN CHAIN F THE M ...THE MODEL IS DERIVED FROM PDB ENTRY 3ZEN BOEHRINGER ET AL., 2013 AND REPRESENTS A RIGID BODY DOCKING OF THE MODEL INTO A CRYO-EM MAP. IN CHAIN F THE MAT AND DH DOMAINS WHERE FIT INDEPENDENTLY OF THE REST OF THE MODEL. IN CHAIN D, RESIDUES 1- 400 (AT DOMAIN) WERE DELETED AS THE DENSITY OF THE EM MAP IN THAT REGION IS FRAGMENTED DUE TO FLEXIBILITY. SUBMISSION BASED ON EXPERIMENTAL DATA FROM EMDB EMD-2357. (DEPOSITION ID: 11618).
Refinement Type
Symmetry TypePOINT
Point SymmetryC1
Map-Model Fitting and Refinement
Id1 (3ZEN)
Refinement SpaceREAL
Refinement ProtocolRIGID BODY FIT
Refinement Target
Overall B Value
Fitting Procedure
DetailsMETHOD--RIGID BODY REFINEMENT PROTOCOL--RIGID BODY
Data Acquisition
Detector TypeKODAK SO-163 FILM
Electron Dose (electrons/Å**2)
Imaging Experiment1
Date of Experiment2010-12-16
Temperature (Kelvin)
Microscope ModelFEI POLARA 300
Minimum Defocus (nm)1800
Maximum Defocus (nm)4500
Minimum Tilt Angle (degrees)
Maximum Tilt Angle (degrees)
Nominal CS
Imaging ModeBRIGHT FIELD
Specimen Holder Model
Nominal Magnification59000
Calibrated Magnification
SourceFIELD EMISSION GUN
Acceleration Voltage (kV)200
Imaging Details
EM Software
TaskSoftware PackageVersion
RECONSTRUCTIONEMAN2
RECONSTRUCTIONSPARX