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PDBsum entry 4b0d

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protein links
Hydrolase PDB id
4b0d

 

 

 

 

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Contents
Protein chain
129 a.a.
Waters ×167
PDB id:
4b0d
Name: Hydrolase
Title: Crystal structure of hen egg white lysozyme from an auto harvested crystal
Structure: LysozymE C. Chain: a. Synonym: 1,4-beta-n-acetylmuramidasE C, allergen gal d iv, gal d 4. Ec: 3.2.1.17
Source: Gallus gallus. Chicken. Organism_taxid: 9031
Resolution:
1.10Å     R-factor:   0.187     R-free:   0.208
Authors: F.Cipriani,M.Rower,C.Landret,U.Zander,F.Felisaz,J.A.Marquez
Key ref: F.Cipriani et al. (2012). CrystalDirect: a new method for automated crystal harvesting based on laser-induced photoablation of thin films. Acta Crystallogr D Biol Crystallogr, 68, 1393-1399. PubMed id: 22993093
Date:
02-Jul-12     Release date:   24-Oct-12    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P00698  (LYSC_CHICK) -  Lysozyme C from Gallus gallus
Seq:
Struc:
147 a.a.
129 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.3.2.1.17  - lysozyme.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Hydrolysis of the 1,4-beta-linkages between N-acetyl-D-glucosamine and N-acetylmuramic acid in peptidoglycan heteropolymers of the prokaryotes cell walls.

 

 
Acta Crystallogr D Biol Crystallogr 68:1393-1399 (2012)
PubMed id: 22993093  
 
 
CrystalDirect: a new method for automated crystal harvesting based on laser-induced photoablation of thin films.
F.Cipriani, M.Röwer, C.Landret, U.Zander, F.Felisaz, J.A.Márquez.
 
  ABSTRACT  
 
The use of automated systems for crystallization and X-ray data collection is now widespread. However, these two steps are separated by the need to transfer crystals from crystallization supports to X-ray data-collection supports, which is a difficult manual operation. Here, a new approach is proposed called CrystalDirect (CD) which enables full automation of the crystal-harvesting process. In this approach, crystals are grown on ultrathin films in a newly designed vapour-diffusion crystallization plate and are recovered by excision of the film through laser-induced photoablation. The film pieces containing crystals are then directly attached to a pin for X-ray data collection. This new method eliminates the delicate step of `crystal fishing', thereby enabling full automation of the crystal-mounting process. Additional advantages of this approach include the absence of mechanical stress and that it facilitates handling of microcrystals. The CD crystallization plates are also suitable for in situ crystal screening with minimal X-ray background. This method could enable the operational integration of highly automated crystallization and data-collection facilities, minimizing the delay between crystal identification and diffraction measurements. It can also contribute significantly to the advancement of challenging projects that require the systematic testing of large numbers of crystals.
 

 

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