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PDBsum entry 6mh6

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protein ligands metals links
Hydrolase PDB id
6mh6

 

 

 

 

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Contents
Protein chain
279 a.a.
Ligands
NO3
Metals
_CA ×2
Waters ×137
PDB id:
6mh6
Name: Hydrolase
Title: High-viscosity injector-based pink beam serial crystallography of micro-crystals at a synchrotron radiation source.
Structure: Proteinase k. Chain: a. Synonym: endopeptidase k,tritirachium alkaline proteinase. Engineered: yes
Source: Synthetic: yes. Parengyodontium album. Organism_taxid: 37998
Resolution:
1.80Å     R-factor:   0.134     R-free:   0.175
Authors: J.M.Martin-Garcia,L.Zhu,D.Mendez,M.Lee,E.Chun,C.Li,H.Hu, G.Subramanian,D.Kissick,C.Ogata,R.Henning,A.Ishchenko,Z.Dobson, S.Zhan,U.Weierstall,J.C.H.Spence,P.Fromme,N.A.Zatsepin, R.F.Fischetti,V.Cherezov,W.Liu
Key ref: J.M.Martin-Garcia et al. (2019). High-viscosity injector-based pink-beam serial crystallography of microcrystals at a synchrotron radiation source. IUCrJ, 6, 412-425. PubMed id: 31098022 DOI: 10.1107/S205225251900263X
Date:
17-Sep-18     Release date:   24-Apr-19    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P06873  (PRTK_PARAQ) -  Proteinase K from Parengyodontium album
Seq:
Struc:
384 a.a.
279 a.a.*
Key:    PfamA domain  Secondary structure
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class: E.C.3.4.21.64  - peptidase K.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Hydrolysis of keratin and of other proteins, with subtilisin-like specificity. Hydrolyzes peptides amides.

 

 
DOI no: 10.1107/S205225251900263X IUCrJ 6:412-425 (2019)
PubMed id: 31098022  
 
 
High-viscosity injector-based pink-beam serial crystallography of microcrystals at a synchrotron radiation source.
J.M.Martin-Garcia, L.Zhu, D.Mendez, M.Y.Lee, E.Chun, C.Li, H.Hu, G.Subramanian, D.Kissick, C.Ogata, R.Henning, A.Ishchenko, Z.Dobson, S.Zhang, U.Weierstall, J.C.H.Spence, P.Fromme, N.A.Zatsepin, R.F.Fischetti, V.Cherezov, W.Liu.
 
  ABSTRACT  
 
Since the first successful serial crystallography (SX) experiment at a synchrotron radiation source, the popularity of this approach has continued to grow showing that third-generation synchrotrons can be viable alternatives to scarce X-ray free-electron laser sources. Synchrotron radiation flux may be increased ∼100 times by a moderate increase in the bandwidth ('pink beam' conditions) at some cost to data analysis complexity. Here, we report the first high-viscosity injector-based pink-beam SX experiments. The structures of proteinase K (PK) and A2A adenosine receptor (A2AAR) were determined to resolutions of 1.8 and 4.2 Å using 4 and 24 consecutive 100 ps X-ray pulse exposures, respectively. Strong PK data were processed using existing Laue approaches, while weaker A2AAR data required an alternative data-processing strategy. This demonstration of the feasibility presents new opportunities for time-resolved experiments with microcrystals to study structural changes in real time at pink-beam synchrotron beamlines worldwide.
 

 

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