7A42

Fluoroacetate Dehalogenase measured by serial synchrotron crystallography


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.75 Å
  • R-Value Free: 0.193 
  • R-Value Work: 0.157 
  • R-Value Observed: 0.158 

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Literature

Serial femtosecond and serial synchrotron crystallography can yield data of equivalent quality: A systematic comparison.

Mehrabi, P.Bucker, R.Bourenkov, G.Ginn, H.M.von Stetten, D.Muller-Werkmeister, H.M.Kuo, A.Morizumi, T.Eger, B.T.Ou, W.L.Oghbaey, S.Sarracini, A.Besaw, J.E.Pare-Labrosse, O.Meier, S.Schikora, H.Tellkamp, F.Marx, A.Sherrell, D.A.Axford, D.Owen, R.L.Ernst, O.P.Pai, E.F.Schulz, E.C.Miller, R.J.D.

(2021) Sci Adv 7

  • DOI: 10.1126/sciadv.abf1380
  • Primary Citation of Related Structures:  
    7A42, 7A43, 7A44, 7A45

  • PubMed Abstract: 
  • For the two proteins myoglobin and fluoroacetate dehalogenase, we present a systematic comparison of crystallographic diffraction data collected by serial femtosecond (SFX) and serial synchrotron crystallography (SSX). To maximize comparability, we used the same batch of micron-sized crystals, the same sample delivery device, and the same data analysis software ...

    For the two proteins myoglobin and fluoroacetate dehalogenase, we present a systematic comparison of crystallographic diffraction data collected by serial femtosecond (SFX) and serial synchrotron crystallography (SSX). To maximize comparability, we used the same batch of micron-sized crystals, the same sample delivery device, and the same data analysis software. Overall figures of merit indicate that the data of both radiation sources are of equivalent quality. For both proteins, reasonable data statistics can be obtained with approximately 5000 room-temperature diffraction images irrespective of the radiation source. The direct comparability of SSX and SFX data indicates that the quality of diffraction data obtained from these samples is linked to the properties of the crystals rather than to the radiation source. Therefore, for other systems with similar properties, time-resolved experiments can be conducted at the radiation source that best matches the desired time resolution.


    Organizational Affiliation

    Department of Physics, Universität Hamburg, Jungiusstrasse 9, 20355 Hamburg, Germany.



Macromolecules
Find similar proteins by:  (by identity cutoff)  |  Structure
Entity ID: 1
MoleculeChainsSequence LengthOrganismDetailsImage
Fluoroacetate dehalogenaseA, B306Rhodopseudomonas palustrisMutation(s): 0 
Gene Names: RPA1163
EC: 3.8.1.3
UniProt
Find proteins for Q6NAM1 (Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009))
Explore Q6NAM1 
Go to UniProtKB:  Q6NAM1
Protein Feature View
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  • Reference Sequence
Small Molecules
Ligands 1 Unique
IDChainsName / Formula / InChI Key2D Diagram3D Interactions
CL (Subject of Investigation/LOI)
Query on CL

Download Ideal Coordinates CCD File 
C [auth A], D [auth B]CHLORIDE ION
Cl
VEXZGXHMUGYJMC-UHFFFAOYSA-M
 Ligand Interaction
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.75 Å
  • R-Value Free: 0.193 
  • R-Value Work: 0.157 
  • R-Value Observed: 0.158 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 41.9α = 90
b = 79.9β = 103.4
c = 84.8γ = 90
Software Package:
Software NamePurpose
PHENIXrefinement
CrystFELdata reduction
PHASERphasing

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2021-04-07
    Type: Initial release