5ANG

Crystal structure of CDK2 in complex with 7-hydroxy-4-(morpholinomethyl)chromen-2-one processed with the CrystalDirect automated mounting and cryo-cooling technology


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.90 Å
  • R-Value Free: 0.236 
  • R-Value Work: 0.197 
  • R-Value Observed: 0.199 

wwPDB Validation   3D Report Full Report


Ligand Structure Quality Assessment 


This is version 1.2 of the entry. See complete history


Literature

Automated Harvesting and Processing of Protein Crystals Through Laser Photoablation.

Zander, U.Hoffmann, G.Cornaciu, I.Marquette, J.-P.Papp, G.Landret, C.Seroul, G.Sinoir, J.Roewer, M.Felisaz, F.Rodriguez-Puente, S.Mariaule, V.Murphy, P.Mathieu, M.Cipriani, F.Marquez, J.A.

(2016) Acta Crystallogr D Biol Crystallogr 72: 454

  • DOI: https://doi.org/10.1107/S2059798316000954
  • Primary Citation of Related Structures:  
    5AMW, 5AMX, 5AMZ, 5AN4, 5AND, 5ANE, 5ANG, 5ANI, 5ANJ, 5ANK, 5ANL, 5ANO, 5DWP, 5EBH

  • PubMed Abstract: 

    Currently, macromolecular crystallography projects often require the use of highly automated facilities for crystallization and X-ray data collection. However, crystal harvesting and processing largely depend on manual operations. Here, a series of new methods are presented based on the use of a low X-ray-background film as a crystallization support and a photoablation laser that enable the automation of major operations required for the preparation of crystals for X-ray diffraction experiments. In this approach, the controlled removal of the mother liquor before crystal mounting simplifies the cryocooling process, in many cases eliminating the use of cryoprotectant agents, while crystal-soaking experiments are performed through diffusion, precluding the need for repeated sample-recovery and transfer operations. Moreover, the high-precision laser enables new mounting strategies that are not accessible through other methods. This approach bridges an important gap in automation and can contribute to expanding the capabilities of modern macromolecular crystallography facilities.


  • Organizational Affiliation

    Grenoble Outstation, European Molecular Biology Laboratory; Unit of Virus Host-Cell Interactions (UMI 3265), University Grenoble Alpes-EMBL-CNRS, 71 Avenue des Martyrs, 38042 Grenoble, France.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
CYCLIN-DEPENDENT KINASE 2298Homo sapiensMutation(s): 0 
EC: 2.7.11.22
UniProt & NIH Common Fund Data Resources
Find proteins for P24941 (Homo sapiens)
Explore P24941 
Go to UniProtKB:  P24941
PHAROS:  P24941
GTEx:  ENSG00000123374 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP24941
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
WY3
Query on WY3

Download Ideal Coordinates CCD File 
B [auth A]7-HYDROXY-4-(MORPHOLINOMETHYL)CHROMEN-2-ONE
C14 H15 N O4
LLQWUZKGZZNBKG-UHFFFAOYSA-N
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.90 Å
  • R-Value Free: 0.236 
  • R-Value Work: 0.197 
  • R-Value Observed: 0.199 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 53.711α = 90
b = 71.828β = 90
c = 72.351γ = 90
Software Package:
Software NamePurpose
REFMACrefinement

Structure Validation

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Ligand Structure Quality Assessment 


Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2016-04-13
    Type: Initial release
  • Version 1.1: 2016-04-20
    Changes: Database references
  • Version 1.2: 2019-04-24
    Changes: Data collection, Other, Source and taxonomy