2PZ9

Crystal structure of putative transcriptional regulator SCO4942 from Streptomyces coelicolor


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.80 Å
  • R-Value Free: 0.269 
  • R-Value Work: 0.213 
  • R-Value Observed: 0.216 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

In situ proteolysis for protein crystallization and structure determination.

Dong, A.Xu, X.Edwards, A.M.Chang, C.Chruszcz, M.Cuff, M.Cymborowski, M.Di Leo, R.Egorova, O.Evdokimova, E.Filippova, E.Gu, J.Guthrie, J.Ignatchenko, A.Joachimiak, A.Klostermann, N.Kim, Y.Korniyenko, Y.Minor, W.Que, Q.Savchenko, A.Skarina, T.Tan, K.Yakunin, A.Yee, A.Yim, V.Zhang, R.Zheng, H.Akutsu, M.Arrowsmith, C.Avvakumov, G.V.Bochkarev, A.Dahlgren, L.G.Dhe-Paganon, S.Dimov, S.Dombrovski, L.Finerty, P.Flodin, S.Flores, A.Graslund, S.Hammerstrom, M.Herman, M.D.Hong, B.S.Hui, R.Johansson, I.Liu, Y.Nilsson, M.Nedyalkova, L.Nordlund, P.Nyman, T.Min, J.Ouyang, H.Park, H.W.Qi, C.Rabeh, W.Shen, L.Shen, Y.Sukumard, D.Tempel, W.Tong, Y.Tresagues, L.Vedadi, M.Walker, J.R.Weigelt, J.Welin, M.Wu, H.Xiao, T.Zeng, H.Zhu, H.

(2007) Nat Methods 4: 1019-1021

  • DOI: https://doi.org/10.1038/nmeth1118
  • Primary Citation of Related Structures:  
    2PZ9

  • PubMed Abstract: 

    We tested the general applicability of in situ proteolysis to form protein crystals suitable for structure determination by adding a protease (chymotrypsin or trypsin) digestion step to crystallization trials of 55 bacterial and 14 human proteins that had proven recalcitrant to our best efforts at crystallization or structure determination. This is a work in progress; so far we determined structures of 9 bacterial proteins and the human aminoimidazole ribonucleotide synthetase (AIRS) domain.


  • Organizational Affiliation

    Structural Genomics Consortium, University of Toronto, 100 College Street, Toronto, Ontario M5G 1L5, Canada.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Putative regulatory protein226Streptomyces coelicolor A3(2)Mutation(s): 0 
Gene Names: SCO49422SCK31.02c
UniProt
Find proteins for Q9EWE9 (Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145))
Explore Q9EWE9 
Go to UniProtKB:  Q9EWE9
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ9EWE9
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.80 Å
  • R-Value Free: 0.269 
  • R-Value Work: 0.213 
  • R-Value Observed: 0.216 
  • Space Group: P 32 2 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 66.96α = 90
b = 66.96β = 90
c = 104.345γ = 120
Software Package:
Software NamePurpose
HKL-2000data collection
HKL-2000data reduction
HKL-3000phasing
MLPHAREphasing
DMmodel building
SHELXDphasing
Omodel building
SOLVEphasing
SHELXEmodel building
RESOLVEmodel building
Cootmodel building
CCP4model building
REFMACrefinement
ADSCdata collection
HKL-2000data scaling
DMphasing
RESOLVEphasing
CCP4phasing

Structure Validation

View Full Validation Report



Entry History 

Revision History  (Full details and data files)

  • Version 1.0: 2007-06-19
    Type: Initial release
  • Version 1.1: 2007-11-14
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Advisory, Derived calculations, Version format compliance
  • Version 1.3: 2022-04-13
    Changes: Database references, Derived calculations, Structure summary