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Multiple distinct assemblies reveal conformational flexibility in the small heat shock protein Hsp26.

by single particle reconstruction, at 14.2 A resolution

Movie

Orientation:

#1: Surface view with section colored by density value, Surface level: 0.035471745, Made by UCSF CHIMERA

#2: Surface view colored by radius, Surface level: 0.035471745, Made by UCSF CHIMERA

Entry
Summary
Database / IDEM DATA BANK (EMDB) / 1227
TitleMultiple distinct assemblies reveal conformational flexibility in the small heat shock protein Hsp26.
MapSurface view of the compact form of a variant form of yeast Hsp26
SampleHsp26, DeltaN1-30 truncation
AuthorsWhite HE, Orlova EV, Chen S, Wang L, Ignatiou A, Gowen B, Stromer T, Franzmann TM, Haslbeck M, Buchner J, Saibil HR
DateDeposition: 2006-05-09, Header release: 2006-05-24, Map release: 2006-07-25, Last update: 2011-05-26
EMDB SitesEMDB @PDBe (EU), EMDB @RCSB (USA)
Structure Visualization
MoviesMovie Page

#1: Surface view with section colored by density value, Surface level: 0.035471745, Made by UCSF CHIMERA

#2: Surface view colored by radius, Surface level: 0.035471745, Made by UCSF CHIMERA

Supplemental images
Structure viewersYorodumi, Launch PeppeR (About PeppeR), Volume viewer (RCSB, PDBe)
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Similar strucutres (beta)
List of similar structure data about Omokage system
Article
Citation - Primary
ArticleStructure, Vol. 14, Issue 7, Page 1197-204, Year 2006
TitleMultiple distinct assemblies reveal conformational flexibility in the small heat shock protein Hsp26.
AuthorsHelen E White, Elena V Orlova, Shaoxia Chen, Luchun Wang, Athanasios Ignatiou, Brent Gowen, Thusnelda Stromer, Titus M Franzmann, Martin Haslbeck, Johannes Buchner, Helen R Saibil
Department of Crystallography, Birkbeck College, London WC1E 7HX, United Kingdom.
KeywordsBinding Sites, Cryoelectron Microscopy, Dimerization, HSP26 protein, S cerevisiae, Heat-Shock Proteins (chemistry), Protein Structure, Quaternary, Saccharomyces cerevisiae Proteins (chemistry), alpha-Crystallins (chemistry)
LinksPII: S0969-2126(06)00260-7, DOI: 10.1016/j.str.2006.05.021, PubMed: 16843901
Map
FileEMD-1227.map ( map file in CCP4 format, 8389 KB )
Projections & SlicesSize of images:
AxesZ (Sec.)X (Row.)Y (Col.)
Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider package.

Density
Contour Level:0.0254, 0.0354717 (movie #1):
Minimum - Maximum: -0.0424559 - 0.218115
Average (Standard dev.): 0.00389035 (0.0189218)
Data Typefloat (32-bit)
Space Group Number1
Map Geometry
Axis Order : Y X Z
Dimensions : 128 128 128
Origin : -64 -64 -64
Limit : 63 63 63
Spacing : 128 128 128
Unit CellA = 238.08 A , B = 238.08 A , C = 238.08 A ,
alpha =
90 degrees , beta = 90 degrees , gamma = 90 degrees
Pixel SpacingX = 1.86 A , Y = 1.86 A , Z = 1.86 A
CCP4 map header info
modeImage stored as Reals
A/pix X/Y/Z1.861.861.86
M x/y/z128128128
origin x/y/z0.0000.0000.000
length x/y/z238.080238.080238.080
alpha/beta/gamma90.00090.00090.000
start NX/NY/NZ-64-64-64
NX/NY/NZ128128128
MAP C/R/S213
start NC/NR/NS-64-64-64
NC/NR/NS128128128
start NC,NX/NR,NY/NS,NZ111
NC,NX/NR,NY/NS,NZ646464
D min/max/mean-0.0420.2180.004
Annotation DetailsSurface view of the compact form of a variant form of yeast Hsp26
Supplement
Images
Images
Sample
NameHsp26, DeltaN1-30 truncation
Oligomeric State24-mer
Number of Components1
Component #1: protein - Hsp26
Scientific nameHsp26
Oligomeric Details24-mer
Number of Copies1
Scientific Name of SpeciesSaccharomyces cerevisiae (NCBI Taxonomy: 4932)

Common Name of Speciesyeast
Recombinant expressionYes
Engineered SourceExp System: Saccharomyces cerevisiae (NCBI Taxonomy: 4932)
Experiment
Sample Preparation
Specimen Conc0.7 mg/ml
Specimen Stateparticle
BufferDetails: 20 mM Hepes/KOH, 50 mM KCl, 5 mM EDTA, 1 mM DTT
pH: 7.5
Vitrification
Cryogen NameETHANE
Imaging
MicroscopeFEI TECNAI F20
Electron Gun
Electron SourceFIELD EMISSION GUN
Accelerating Voltage200 kV
Illumination ModeFLOOD BEAM
Lens
MagnificationNominal: 50000 X,
Imaging ModeBRIGHT FIELD
Defocus1700 nm - 3400 nm
Specimen Holder
HolderEucentric ( GATAN LIQUID NITROGEN )
Camera
Image Acquisition
Number of Digital Images68
Sampling Size1.4 microns
ScannerZEISS SCAI
Processing
Methodsingle particle reconstruction
3 D reconstruction
AlgorithmAngular reconstitution
SoftwareImagic
CTF CorrectionPhase flipping
Resolution By Author14.2
Resolution MethodFSC at 0.5 cut-off
DetailsAngular reconstitution
Single Particle
Number of Class Averages625
Number of Projections4300
Atomic Model Fitting
Model #0
Refinement Protocolrigid body
SoftwareURO
Refinement SpaceRECIPROCAL
DetailsProtocol: Rigid Body. The alpha crystallin domain dimers were fitted manually into the same region of density observed in the WT maps prior to refinement in URO
Download
Data from EMDB
Header (meta data in XML format)emd-1227.xml (6.8 KB)
Map dataemd_1227.map.gz (781.6 KB)
Images1227.gif (57.3 KB)
FTP directoryftp://ftp.pdbj.org/pub/emdb/structures/EMD-1227
Movie files
movie #1
.mp4 (H.264/MPEG-4 AVC format), 3.3 MB
.webm (WebM/VP8 format), 5.2 MB
Session file for UCSF-Chimera, 19.4 KB
movie #2
.mp4 (H.264/MPEG-4 AVC format), 3.1 MB
.webm (WebM/VP8 format), 4.3 MB
Session file for UCSF-Chimera, 19.6 KB