4WOB

Proteinase-K Pre-Surface Acoustic Wave

  • Classification: HYDROLASE
  • Organism(s): Parengyodontium album
  • Expression System: Tritirachium
  • Mutation(s): No 

  • Deposited: 2014-10-15 Released: 2015-02-18 
  • Deposition Author(s): French, J.B.
  • Funding Organization(s): National Institutes of Health/Office of the Director, National Science Foundation (NSF, United States)

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.90 Å
  • R-Value Free: 0.257 
  • R-Value Work: 0.188 
  • R-Value Observed: 0.195 

wwPDB Validation   3D Report Full Report


This is version 2.2 of the entry. See complete history


Literature

Precise Manipulation and Patterning of Protein Crystals for Macromolecular Crystallography Using Surface Acoustic Waves.

Guo, F.Zhou, W.Li, P.Mao, Z.Yennawar, N.H.French, J.B.Huang, T.J.

(2015) Small 11: 2733-2737

  • DOI: https://doi.org/10.1002/smll.201403262
  • Primary Citation of Related Structures:  
    4WO6, 4WO9, 4WOA, 4WOB, 4WOC

  • PubMed Abstract: 

    Advances in modern X-ray sources and detector technology have made it possible for crystallographers to collect usable data on crystals of only a few micrometers or less in size. Despite these developments, sample handling techniques have significantly lagged behind and often prevent the full realization of current beamline capabilities. In order to address this shortcoming, a surface acoustic wave-based method for manipulating and patterning crystals is developed. This method, which does not damage the fragile protein crystals, can precisely manipulate and pattern micrometer and submicrometer-sized crystals for data collection and screening. The technique is robust, inexpensive, and easy to implement. This method not only promises to significantly increase efficiency and throughput of both conventional and serial crystallography experiments, but will also make it possible to collect data on samples that were previously intractable.


  • Organizational Affiliation

    Department of Engineering Science and Mechanics, The Pennsylvania State University, University Park, PA, 16802, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Proteinase K279Parengyodontium albumMutation(s): 0 
Gene Names: PROK
EC: 3.4.21.64
UniProt
Find proteins for P06873 (Parengyodontium album)
Explore P06873 
Go to UniProtKB:  P06873
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP06873
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
SO4
Query on SO4

Download Ideal Coordinates CCD File 
B [auth A]SULFATE ION
O4 S
QAOWNCQODCNURD-UHFFFAOYSA-L
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.90 Å
  • R-Value Free: 0.257 
  • R-Value Work: 0.188 
  • R-Value Observed: 0.195 
  • Space Group: P 43 21 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 67.84α = 90
b = 67.84β = 90
c = 106.721γ = 90
Software Package:
Software NamePurpose
PHENIXrefinement
PDB_EXTRACTdata extraction

Structure Validation

View Full Validation Report



Entry History & Funding Information

Deposition Data

  • Released Date: 2015-02-18 
  • Deposition Author(s): French, J.B.

Funding OrganizationLocationGrant Number
National Institutes of Health/Office of the DirectorUnited States1DP2OD007209-01
National Science Foundation (NSF, United States)United StatesCBET-1438126 and IIP-1346440

Revision History  (Full details and data files)

  • Version 1.0: 2015-02-18
    Type: Initial release
  • Version 1.1: 2015-07-01
    Changes: Database references
  • Version 1.2: 2017-09-20
    Changes: Author supporting evidence, Derived calculations, Other, Source and taxonomy, Structure summary
  • Version 2.0: 2018-07-25
    Changes: Atomic model, Data collection, Database references, Refinement description, Source and taxonomy
  • Version 2.1: 2019-11-27
    Changes: Author supporting evidence
  • Version 2.2: 2023-12-27
    Changes: Data collection, Database references