SASDCT5: SAXS on intact Doryteuthis squid lens 40% layer (S-crystallin, Q2...

Basic information

• Entry: Database: SASBDB / ID: SASDCT5

Sample

SAXS on intact Doryteuthis squid lens 40% layer

• S-crystallin, Q25367_DOROP (protein), S-crystallin, Q25367, Doryteuthis pealeii

Function / homology

Function:

glutathione metabolic process

Domain/homology:

S-crystallin / Glutathione S-transferase, C-terminal domain / Glutathione S-transferase, N-terminal domain / Glutathione transferase family / Glutathione S-transferase, C-terminal / Glutathione S-transferase, C-terminal-like / Soluble glutathione S-transferase C-terminal domain profile. / Soluble glutathione S-transferase N-terminal domain profile. / Glutathione S-transferase, N-terminal / Glutathione S-transferase, C-terminal domain superfamily / Thioredoxin-like superfamily

Component:

S-crystallin

• Biological species: Doryteuthis pealeii (longfin inshore squid)
• Citation: Journal: Science / Year: 2017; Title: Eye patches: Protein assembly of index-gradient squid lenses.; Authors: J Cai / J P Townsend / T C Dodson / P A Heiney / A M Sweeney / ; Abstract: A parabolic relationship between lens radius and refractive index allows spherical lenses to avoid spherical aberration. We show that in squid, patchy colloidal physics resulted from an evolutionary radiation of globular S-crystallin proteins. Small-angle x-ray scattering experiments on lens tissue show colloidal gels of S-crystallins at all radial positions. Sparse lens materials form via low-valence linkages between disordered loops protruding from the protein surface. The loops are polydisperse and bind via a set of hydrogen bonds between disordered side chains. Peripheral lens regions with low particle valence form stable, volume-spanning gels at low density, whereas central regions with higher average valence gel at higher densities. The proteins demonstrate an evolved set of linkers for self-assembly of nanoparticles into volumetric materials.

Contact author

• Jing Cai (Penn, University of Pennsylvania, Philadelphia, PA, United States)

Models

• Model #1364: ; Type: dummy / Software: (1.1.2) / Radius of dummy atoms: 4.20 A / Symmetry: None / Comment: An invert method has been applied. / Chi-square value: 2.765569; Search similar-shape structures of this assembly by Omokage search (details)

Sample

• Sample: Name: SAXS on intact Doryteuthis squid lens 40% layer
• Buffer: Name: Tissue fluid / pH: 7

Entity #672

Name: S-crystallin, Q25367 / Type: protein / Description: S-crystallin, Q25367_DOROP / Formula weight: 27.289 / Num. of mol.: 2 / Source: Doryteuthis pealeii / References: UniProt: Q25367_DOR
Sequence:

MPTYTLYYFN GRGRAEVLRM MFAAANVKYM DKRFEFNEWD KYRKDMPSMC VPVLEMDGGN KMPETMAIPR YLAREFGFYG KSNMDMMRCD YIADCFYEIM HDYMRYFHEK NGRFRSSMEG SGNGMNSPTG ASGDMNSNSN FDTYLQWRFM NTCNRVLPFL ERTLEMQNGG KAFFMGDQMM WCDMMCHCAL EGPFMENQSM LSKHPKLMAL RTRIASHPKI SGYLKSRSNT NW

Experimental information

• Beam: Instrument name: National Synchrotron Light Source (NSLS) X9A; City: Brookhaven, NY / 国: USA / Type of source: X-ray synchrotron / Wavelength: 0.1 Å
• Detector: Name: Pilatus 300K / Type: 20Hz

Scan

Title: SAXS on intact Doryteuthis squid lens 40% layer / Measurement date: Jul 17, 2014 / Storage temperature: 10 °C / Cell temperature: 10 °C / Exposure time: 300 sec. / Number of frames: 1 / Unit: 1/A /

	Min	Max
Q	0.004	1

• Result: Experimental MW: 50 kDa / I0 from PR: 180 / Rg from PR: 2.4 nm / Type of curve: single_conc; Comments: The space-filling model ultimately represents the spatial density fluctuation of the material, not the presence of material. Since we measured a nearly water-free density of material at the core of the lens, we show the void density of the model prediction here.