|Entry||Database: EMDB / ID: 2289|
|Title||Second 3D model of wild type MjHSP16.5 at room temperature by CryoEM.|
|Map data||Second model for reconstruction of wild type MjHSP16.5 at room temperature|
|Sample||wild type small heat shock protein (sHSP) HSP16.5 from Methanocaldococcus jannaschii (MjHSP16.5):|
|Keywords||Small heat shock protein / HSP16.5|
|Function / homology||Alpha crystallin/Hsp20 domain / HSP20-like chaperone / Hsp20/alpha crystallin family / Small heat shock protein (sHSP) domain profile. / Alpha crystallin/Hsp20 domain / HSP20-like chaperone / response to stress / protein stabilization / protein homooligomerization / protein-containing complex ...Alpha crystallin/Hsp20 domain / HSP20-like chaperone / Hsp20/alpha crystallin family / Small heat shock protein (sHSP) domain profile. / Alpha crystallin/Hsp20 domain / HSP20-like chaperone / response to stress / protein stabilization / protein homooligomerization / protein-containing complex / identical protein binding / cytoplasm / Small heat shock protein HSP16.5|
Function and homology information
|Source||Methanocaldococcus jannaschii (archaea)|
|Method||single particle reconstruction / cryo EM / 12 Å resolution|
|Authors||Roy A Q / Yan Z / Andrew L / Ian W / Ehmke P / Fei S|
|Citation||Journal: Philos. Trans. R. Soc. Lond., B, Biol. Sci. / Year: 2013|
Title: Changes in the quaternary structure and function of MjHSP16.5 attributable to deletion of the IXI motif and introduction of the substitution, R107G, in the α-crystallin domain.
Authors: Roy A Quinlan / Yan Zhang / Andrew Lansbury / Ian Williamson / Ehmke Pohl / Fei Sun
|Date||Deposition: Jan 21, 2013 / Header (metadata) release: Feb 27, 2013 / Map release: Mar 13, 2013 / Last update: Jul 31, 2013|
|Structure viewer||EM map: |
Downloads & links
|File||emd_2289.map.gz (map file in CCP4 format, 65537 KB)|
|Projections & slices|
Images are generated by Spider.
|Voxel size||X=Y=Z: 0.933 Å|
CCP4 map header:
-Entire wild type small heat shock protein (sHSP) HSP16.5 from Methanocal...
|Entire||Name: wild type small heat shock protein (sHSP) HSP16.5 from Methanocaldococcus jannaschii (MjHSP16.5)|
Number of components: 1 / Oligomeric State: 24mer
|Mass||Theoretical: 396 kDa / Experimental: 396 kDa|
-Component #1: protein, MjHSP16.5
|Protein||Name: MjHSP16.5 / a.k.a: small heat shock protein (sHSP) from HSP16.5 / Oligomeric Details: 24mer / Recombinant expression: Yes / Number of Copies: 24|
|Mass||Theoretical: 16.5 kDa / Experimental: 16.5 kDa|
|Source||Species: Methanocaldococcus jannaschii (archaea)|
|Source (engineered)||Expression System: Escherichia coli (E. coli) / Vector: pET23b|
|Source (natural)||Location in cell: cytoplasmic|
|External references||InterPro: Alpha crystallin/Hsp20 domain, HSP20-like chaperone|
UniProt: Small heat shock protein HSP16.5 / Gene Ontology: cytoplasm, response to stress
|Specimen||Specimen state: particle / Method: cryo EM|
|Sample solution||Specimen conc.: 0.8 mg/ml / Buffer solution: 10mM HEPES, 100mM NaCl. / pH: 7.4|
|Support film||GIG holey grids (LifeTrust, China) were treated with a glow discharge machine (Master Plasmer)|
|Vitrification||Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Temperature: 93 K|
Method: The samples were blotted for 2 s with blot force 2 at 100% humidity.
-Electron microscopy imaging
Model: Titan Krios / Image courtesy: FEI Company
|Imaging||Microscope: FEI TITAN KRIOS / Date: Sep 28, 2012|
|Electron gun||Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Electron dose: 20 e/Å2 / Illumination mode: FLOOD BEAM|
|Lens||Magnification: 96000 X (nominal) / Cs: 2.7 mm / Imaging mode: BRIGHT FIELD / Defocus: 2000 - 3000 nm|
|Specimen Holder||Holder: liquid nitrogen cooled / Model: FEI TITAN KRIOS AUTOGRID HOLDER / Temperature: 85 K|
|Camera||Detector: GATAN ULTRASCAN 4000 (4k x 4k)|
|Image acquisition||Number of digital images: 1160 / Bit depth: 32|
Details: Electron micrograph exposures were made with the automatic collection package Leginon.
|Processing||Method: single particle reconstruction / Number of class averages: 193 / Applied symmetry: O (octahedral) / Number of projections: 4356|
Details: The particles were selected using an automatic selection program Gautomatch developed in Fei Sun lab (to be published). Octahedron symmetry were imposed during 3D reconstructing.
|3D reconstruction||Algorithm: projection matching / Software: EMAN1 / CTF correction: Each image|
Details: The final reconstructed density map was further sharpened by application of an amplitude correction algorithm in the program BFACTOR.
Resolution: 12 Å / Resolution method: FSC 0.5
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