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Structure of the Nuclear Chaperone Nucleoplamsin.

by single particle reconstruction, at 21 A resolution

Movie

Orientation:

#1: Surface view with section colored by density value, Surface level: 0.0225, Made by UCSF CHIMERA

#2: Surface view colored by cylindrical radius, Surface level: 0.0225, Made by UCSF CHIMERA

Entry
Summary
Database / IDEM DATA BANK (EMDB) / 1778
TitleStructure of the Nuclear Chaperone Nucleoplamsin.
MapThis a map of the nuclear chaperone nucleoplasmin.
SampleNucleoplasmin chaperone
KeywordsNucleoplasmin, Histone H2A, Histone H2B, Chaperone, Chromatin, Nuclear-chaperone, Histone-chaperone
AuthorsRamos I, Martin-Benito J, Finn R, Bretana L, Aloria K, Arizmendi JM, Ausio J, Muga A, Valpuesta JM, Prado A
DateDeposition: 2010-08-31, Header release: 2010-10-26, Map release: 2010-10-26, Last update: 2010-10-26
EMDB SitesEMDB @PDBe (EU), EMDB @RCSB (USA)
Structure Visualization
MoviesMovie Page

#1: Surface view with section colored by density value, Surface level: 0.0225, Made by UCSF CHIMERA

#2: Surface view colored by cylindrical radius, Surface level: 0.0225, Made by UCSF CHIMERA

Supplemental images
Structure viewersYorodumi, Launch PeppeR (About PeppeR), Volume viewer (RCSB, PDBe)
Related Structure Data
Related Entries

Cite: data citing same article

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List of similar structure data about Omokage system
Article
Citation - Primary
ArticleJ. Biol. Chem., Vol. 285, Issue 44, Page 33771-8, Year 2010
TitleNucleoplasmin binds histone H2A-H2B dimers through its distal face.
AuthorsIsbaal Ramos, Jaime Martín-Benito, Ron Finn, Laura Bretaña, Kerman Aloria, Jesús M Arizmendi, Juan Ausió, Arturo Muga, José M Valpuesta, Adelina Prado
Departamento de Bioquímica y Biología Molecular, Facultad de Ciencia y Tecnología, Universidad del País Vasco, 48080 Bilbao, Spain.
KeywordsAnimals, Dimerization, Histones (chemistry), Mass Spectrometry (methods), Microscopy, Electron (methods), Nucleoplasmins (chemistry), Phosphorylation, Protein Folding, Protein Interaction Mapping, Protein Structure, Tertiary, Xenopus laevis (metabolism)
LinksDOI: 10.1074/jbc.M110.150664, PubMed: 20696766, PMC: PMC2962476
Map
FileEMD-1778.map ( map file in CCP4 format, 2050 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:0.0225 (by author), 0.0225 (movie #1):
Minimum - Maximum: -0.0623846 - 0.089064
Average (Standard dev.): -0.000197456 (0.00908658)
Data TypeImage stored as Reals
Space Group Number1
Map Geometry
Axis orderXYZ
Dimensions808080
Origin000
Limit797979
Spacing808080
Unit CellA= B= C: 184 A
Alpha=beta=gamma: 90 degrees
Pixel SpacingX= Y= Z: 2.3 A
CCP4 map header info
modeImage stored as Reals
A/pix X/Y/Z2.32.32.3
M x/y/z808080
origin x/y/z0.0000.0000.000
length x/y/z184.000184.000184.000
alpha/beta/gamma90.00090.00090.000
start NX/NY/NZ-184-184-183
NX/NY/NZ368368368
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS808080
start NC,NX/NR,NY/NS,NZ
NC,NX/NR,NY/NS,NZ
D min/max/mean-0.0620.089-0.000
Annotation DetailsThis a map of the nuclear chaperone nucleoplasmin.
Supplement
Images
Images
Sample
NameNucleoplasmin chaperone
Number of Components1
Oligomeric StatePentameric
Theoretical Mass0.11MDa
Experimental Mass0.11MDa
Component #1: protein - Nucleoplasmin
Scientific nameNucleoplasmin
Theoretical Mass0.11 MDa
Experimental Mass0.11 MDa
Oligomeric DetailsPentamer
Number of Copies5
Scientific Name of SpeciesXenopus laevis

Common Name of SpeciesAfrican clawed frog
NCBI taxonomy8355
Recombinant expressionNo
Natural SourceCell: Oocyte
Organ Or Tissue: Egg
Organelle: Nucleus
LinksInter Pro: IPR:004301
Experiment
Sample Preparation
StainingGrids were stained with 2% w/v Uranyl Acetate solution for 1 minute.
Specimen Support Details200 mesh CuRh grid
Specimen Stateparticle
BufferDetails: 2mM MgCl2, 240mM NaCl, 25 mM Tris-HCl
pH: 7.5
Vitrification
Cryogen NameNONE
InstrumentNONE
Imaging
MicroscopeJEOL 1200EXII
Electron Gun
Electron SourceTUNGSTEN HAIRPIN
Accelerating Voltage100 kV
Illumination ModeFLOOD BEAM
Lens
MagnificationNominal: 60000
AstigmatismObjective lens astigmatism was corrected at 200,000 times magnification
Nominal Cs5.6 mm
Imaging ModeBRIGHT FIELD
Defocus1000 nm - 2500 nm
Specimen Holder
HolderEucentric
ModelJEOL
Camera
DetectorKodak SO163 film
Image Acquisition
ScannerZEISS SCAI
Number of Digital Images10
Sampling Size2.3
Quant Bit Number8
Detailsdownsampling factor of 2
Processing
Methodsingle particle reconstruction
3D reconstruction
AlgorithmProjection matching
SoftwareEMAN, XMIPP, SPIDER
CTF CorrectionEach plate
Resolution By Author21 A
Resolution MethodFSC at 0.5 cut-off
Single Particle
Number of Projections9862
Download
Data from EMDB
Header (meta data in XML format)emd-1778.xml (7.2 KB)
Map dataemd_1778.map.gz (1.8 MB)
Imagesimage_EMD1778.tif (756.1 KB)
FTP directoryftp://ftp.pdbj.org/pub/emdb/structures/EMD-1778
Movie files
movie #1
.mp4 (H.264/MPEG-4 AVC format), 3.6 MB
.webm (WebM/VP8 format), 5.4 MB
Session file for UCSF-Chimera, 26.3 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, 26.3 KB