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Nucleotide-induced conformations in the neck region of dimeric kinesin.

by helical reconstruction, at 25 A resolution

Movie

Orientation:

#1: Surface view with section colored by density value, Surface level: 54.470584561, Made by UCSF CHIMERA

#2: Surface view colored by cylindrical radius, Surface level: 54.470584561, Made by UCSF CHIMERA

Entry
Summary
Database / IDEM DATA BANK (EMDB) / 1039
AuthorsSkiniotis G
EMDB SitesEMDB @PDBe (EU), EMDB @RCSB (USA)
Structure Visualization
MoviesMovie Page

#1: Surface view with section colored by density value, Surface level: 54.470584561, Made by UCSF CHIMERA

#2: Surface view colored by cylindrical radius, Surface level: 54.470584561, Made by UCSF CHIMERA

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List of similar structure data about Omokage system
Article
Citation - Primary
ArticleEMBO J., Vol. 22, Issue 7, Page 1518-28, Year 2003
TitleNucleotide-induced conformations in the neck region of dimeric kinesin.
AuthorsGeorgios Skiniotis, Thomas Surrey, Stephan Altmann, Heinz Gross, Young-Hwa Song, Eckhard Mandelkow, Andreas Hoenger
European Molecular Biology Laboratory, Meyerhofstrasse 1, D-69117 Heidelberg, Germany.
KeywordsAdenosine Monophosphate (chemistry, 61-19-8), Cloning, Molecular, Cryoelectron Microscopy, Dimerization, Kinesin (chemistry, 3.6.1.-), Models, Molecular, Protein Conformation, Recombinant Fusion Proteins (chemistry), Recombinant Proteins (chemistry), src Homology Domains
LinksPubMed: 12660159, DOI: 10.1093/emboj/cdg164, PMC: PMC152908
Map
FileEMD-1039.map ( map file in CCP4 format, 4001 KB )
Projections & SlicesSize of images:
AxesZ (Sec.)Y (Row.)X (Col.)
Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider package.

Density
Contour Level:63.6, 54.4705846 (movie #1):
Minimum - Maximum: 0 - 100
Average (Standard dev.): 40.3611 (10.6337)
Data Typefloat (32-bit)
Space Group Number1
Map Geometry
Axis Order : X Y Z
Dimensions : 100 100 100
Origin : 0 0 0
Limit : 99 99 99
Spacing : 100 100 100
Unit CellA = 552.6 A , B = 552.6 A , C = 552.6 A ,
alpha =
90 degrees , beta = 90 degrees , gamma = 90 degrees
Pixel SpacingX = 5.526 A , Y = 5.526 A , Z = 5.526 A
CCP4 map header info
modeImage stored as Reals
A/pix X/Y/Z5.5265.5265.526
M x/y/z100100100
origin x/y/z0.0000.0000.000
length x/y/z552.600552.600552.600
alpha/beta/gamma90.00090.00090.000
start NX/NY/NZ
NX/NY/NZ
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS100100100
start NC,NX/NR,NY/NS,NZ
NC,NX/NR,NY/NS,NZ
D min/max/mean0.000100.00040.361
Annotation Detailsrat kinesin dimer with an SH3 domain cloned within the neck region -rKS379-, complexed to subtilisin treated microtubules in the presence of AMP-PNP
Supplement
Images
Images
Sample
NameRat kinesin dimer with an SH3 domain complexed to subtilisin treated microtubules in the presence of AMP-PNP.
Oligomeric Statedimer
Number of Components2
Component #1: protein - molecular motor
Scientific namerat kinesin
Common Namemolecular motor
Experimental Mass0.98 MDa
Oligomeric Detailsdimer
Number of Copies1
Scientific Name of SpeciesRattus norvegicus (NCBI Taxonomy: 10116)

Common Name of Speciesrat kinesin
Recombinant expressionYes
Engineered SourceExp System: Escherichia coli (NCBI Taxonomy: 562)
Vector: pET3
Component #2: protein - microtubule
Scientific nametubulin
Common Namemicrotubule
Experimental Mass0.11 MDa
Oligomeric Detailshetero-dimer
Number of Copies1
Scientific Name of SpeciesRattus norvegicus (NCBI Taxonomy: 10116)
Common Name of Speciesrat kinesin
Recombinant expressionNo
Natural SourceCell: neuronal cells
Cell Location: cytoplasm
Organ Or Tissue: brain
Experiment
Sample Preparation
Specimen Conc0.5 mg/ml
Stainingice-embeded
Specimen Support Detailsholey grids
Helical ParametersAxial Symmetry: p1
Hand: LEFT HANDED
Specimen Statefilament
BufferDetails: PIPES 80 mM, MgCl2 1 mM, GTP 1 mM, Taxol 20 uM, DMSO 7.5%
pH: 6.8
Vitrification
Cryogen NameETHANE
Temperature93 Kelvin
Imaging
MicroscopeFEI/PHILIPS CM200FEG/ST
Electron Gun
Electron SourceFIELD EMISSION GUN
Accelerating Voltage200 kV
Electron Dose5 e/A**2
Illumination ModeFLOOD BEAM
Lens
MagnificationNominal: 38000 X,
Astigmatismwas corrected at 180,000 times mag.
Nominal Cs2 mm
Imaging ModeBRIGHT FIELD
Defocus2000 nm - 2500 nm
Specimen Holder
Holderside entry ( GATAN LIQUID NITROGEN )
Tilt Angle0 degrees - 0 degrees
Camera
DetectorKodak SO163 film
Image Acquisition
Number of Digital Images12
Sampling Size21 microns
Quant Bit Number8
ScannerZEISS SCAI
Processing
Methodhelical reconstruction
3 D reconstruction
Algorithmlayer lines, Bessel orders
SoftwarePHOELIX, SUPRIM
Resolution By Author25
Resolution MethodFSC at 0.5
DetailsFinal map from 24 averaged datasets = 12 helical tubes
Download
Data from EMDB
Header (meta data in XML format)emd-1039.xml (8 KB)
Map dataemd_1039.map.gz (2.9 MB)
Images1039.gif (65.3 KB)
FTP directoryftp://ftp.pdbj.org/pub/emdb/structures/EMD-1039
Movie files
movie #1
.mp4 (H.264/MPEG-4 AVC format), 3.4 MB
.webm (WebM/VP8 format), 5.4 MB
Session file for UCSF-Chimera, 19.7 KB
movie #2
.mp4 (H.264/MPEG-4 AVC format), 3.2 MB
.webm (WebM/VP8 format), 4.7 MB
Session file for UCSF-Chimera, 19.7 KB