6B6N

Orthorhombic trypsin (295 K) in the presence of 50% mpd

  • Classification: HYDROLASE
  • Organism(s): Bos taurus
  • Expression System: Bos taurus
  • Mutation(s): No 

  • Deposited: 2017-10-03 Released: 2017-11-01 
  • Deposition Author(s): Juers, D.H.
  • Funding Organization(s): National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.00 Å
  • R-Value Free: 0.157 
  • R-Value Work: 0.121 
  • R-Value Observed: 0.122 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

The impact of cryosolution thermal contraction on proteins and protein crystals: volumes, conformation and order.

Juers, D.H.Farley, C.A.Saxby, C.P.Cotter, R.A.Cahn, J.K.B.Holton-Burke, R.C.Harrison, K.Wu, Z.

(2018) Acta Crystallogr D Struct Biol 74: 922-938

  • DOI: https://doi.org/10.1107/S2059798318008793
  • Primary Citation of Related Structures:  
    5UN3, 5UU7, 5UU8, 5UU9, 5UUA, 5UUB, 5UUC, 5UUD, 5UUE, 6AVL, 6B6N, 6B6O, 6B6P, 6B6Q, 6B6R, 6B6S, 6B6T, 6D5N, 6D5O, 6D5P, 6D5Q, 6D5R, 6D5S, 6D5T, 6D5U, 6D6E, 6D6F, 6D6G, 6D6H, 6DZF

  • PubMed Abstract: 

    Cryocooling of macromolecular crystals is commonly employed to limit radiation damage during X-ray diffraction data collection. However, cooling itself affects macromolecular conformation and often damages crystals via poorly understood processes. Here, the effects of cryosolution thermal contraction on macromolecular conformation and crystal order in crystals ranging from 32 to 67% solvent content are systematically investigated. It is found that the solution thermal contraction affects macromolecule configurations and volumes, unit-cell volumes, crystal packing and crystal order. The effects occur through not only thermal contraction, but also pressure caused by the mismatched contraction of cryosolvent and pores. Higher solvent-content crystals are more affected. In some cases the solvent contraction can be adjusted to reduce mosaicity and increase the strength of diffraction. Ice formation in some crystals is found to cause damage via a reduction in unit-cell volume, which is interpreted through solvent transport out of unit cells during cooling. The results point to more deductive approaches to cryoprotection optimization by adjusting the cryosolution composition to reduce thermal contraction-induced stresses in the crystal with cooling.


  • Organizational Affiliation

    Department of Physics, Whitman College, 345 Boyer Avenue, Walla Walla, WA 99362, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Cationic trypsin223Bos taurusMutation(s): 0 
EC: 3.4.21.4
UniProt
Find proteins for P00760 (Bos taurus)
Explore P00760 
Go to UniProtKB:  P00760
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP00760
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.00 Å
  • R-Value Free: 0.157 
  • R-Value Work: 0.121 
  • R-Value Observed: 0.122 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 54.692α = 90
b = 58.538β = 90
c = 67.576γ = 90
Software Package:
Software NamePurpose
CrysalisProdata reduction
SCALAdata scaling
PHENIXrefinement

Structure Validation

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Entry History & Funding Information

Deposition Data

  • Released Date: 2017-11-01 
  • Deposition Author(s): Juers, D.H.

Funding OrganizationLocationGrant Number
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)United States2R15GM090248

Revision History  (Full details and data files)

  • Version 1.0: 2017-11-01
    Type: Initial release
  • Version 1.1: 2017-12-06
    Changes: Author supporting evidence
  • Version 1.2: 2018-09-19
    Changes: Data collection, Database references
  • Version 1.3: 2020-01-01
    Changes: Author supporting evidence