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- PDB-29ik: LASV cap-snatching endonuclease, SFX apo structure -

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Basic information

Entry
Database: PDB / ID: 29ik
TitleLASV cap-snatching endonuclease, SFX apo structure
ComponentsRNA-directed RNA polymerase L
KeywordsHYDROLASE / drug development / Lassa hemorrhagic fever / L protein / Arenaviridae
Function / homology
Function and homology information


negative stranded viral RNA replication / cap snatching / hydrolase activity / host cell / Hydrolases; Acting on ester bonds / nucleotide binding / RNA-directed RNA polymerase / RNA-directed RNA polymerase activity / host cell cytoplasm / metal ion binding
Similarity search - Function
RNA polymerase, arenaviral / RNA endonuclease, cap-snatching / Arenavirus RNA polymerase / Arenavirus cap snatching domain / : / RNA-directed RNA polymerase, negative-strand RNA virus / RdRp of negative ssRNA viruses with segmented genomes catalytic domain profile.
Similarity search - Domain/homology
RNA-directed RNA polymerase L
Similarity search - Component
Biological speciesMammarenavirus lassaense
MethodX-RAY DIFFRACTION / FREE ELECTRON LASER / MOLECULAR REPLACEMENT / Resolution: 2.07 Å
AuthorsFalke, S. / Reinke, P.Y.A. / Senst, J.M. / Lewe, P. / Witt, S. / Meents, A. / Guenther, S.
Funding support Germany, 6items
OrganizationGrant numberCountry
Helmholtz AssociationFISCOV Germany
Helmholtz AssociationFISVIR Germany
Helmholtz AssociationSFragX Germany
Helmholtz AssociationInternLabs-0011-HIR3X Germany
German Federal Ministry for Education and Research13K22CHB Germany
German Federal Ministry for Education and Research16GW0277 Germany
CitationJournal: Acta Crystallogr D Struct Biol / Year: 2026
Title: Perspectives for pharmaceutical screening at XFEL sources using the example of Lassa virus endonuclease.
Authors: Falke, S. / Reinke, P.Y.A. / Rosenberg, D. / Fischer, P. / Meyer, J. / Galchenkova, M. / Tolstikova, A. / Mariani, V. / Senst, J.M. / Lewe, P. / Witt, S. / Wagner, A. / Chapman, H.N. / ...Authors: Falke, S. / Reinke, P.Y.A. / Rosenberg, D. / Fischer, P. / Meyer, J. / Galchenkova, M. / Tolstikova, A. / Mariani, V. / Senst, J.M. / Lewe, P. / Witt, S. / Wagner, A. / Chapman, H.N. / Hunter, M. / Gunther, S. / Meents, A.
History
DepositionMar 13, 2026Deposition site: PDBE / Processing site: PDBE
Revision 1.0Oct 7, 2026Provider: repository / Type: Initial release
Revision 1.1Oct 14, 2026Group: Database references / Category: citation / citation_author
Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation_author.identifier_ORCID

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: RNA-directed RNA polymerase L
hetero molecules


Theoretical massNumber of molelcules
Total (without water)22,9302
Polymers22,9061
Non-polymers241
Water54030
1


  • Idetical with deposited unit
  • defined by author
  • Evidence: gel filtration
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area90 Å2
ΔGint-5 kcal/mol
Surface area9650 Å2
Unit cell
Length a, b, c (Å)58.260, 58.260, 135.380
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number96
Space group name H-MP43212
Space group name HallP4nw2abw
Symmetry operation#1: x,y,z
#2: -y+1/2,x+1/2,z+3/4
#3: y+1/2,-x+1/2,z+1/4
#4: x+1/2,-y+1/2,-z+1/4
#5: -x+1/2,y+1/2,-z+3/4
#6: -x,-y,z+1/2
#7: y,x,-z
#8: -y,-x,-z+1/2

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Components

#1: Protein RNA-directed RNA polymerase L / Protein L / Large structural protein / Replicase / Transcriptase


Mass: 22906.141 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mammarenavirus lassaense / Production host: Escherichia coli BL21(DE3) (bacteria)
References: UniProt: Q6GWS2, RNA-directed RNA polymerase, Hydrolases; Acting on ester bonds
#2: Chemical ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Mg
#3: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 30 / Source method: isolated from a natural source / Formula: H2O
Has ligand of interestN
Has protein modificationY

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

CrystalDensity Matthews: 2.51 Å3/Da / Density % sol: 50.95 %
Crystal growTemperature: 293 K / Method: batch mode
Details: After limited proteolysis with subtilisin A, 7.5 mg/ml target protein were mixed with an equal volume of crystallization solution (10% w/v PEG 10000, 250 mM MgSO4 and 100 mM Tris/HCl pH 9.0)

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Data collection

DiffractionMean temperature: 293 K / Serial crystal experiment: Y
Diffraction sourceSource: FREE ELECTRON LASER / Site: SLAC LCLS / Beamline: MFX / Wavelength: 1.265 Å
DetectorType: SLAC ePix10k 2M / Detector: PIXEL / Date: Oct 15, 2024
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.265 Å / Relative weight: 1
ReflectionResolution: 2.07→21.04 Å / Num. obs: 14959 / % possible obs: 100 % / Redundancy: 732.8 % / Biso Wilson estimate: 43.3 Å2 / CC1/2: 0.967 / CC star: 0.992 / Net I/σ(I): 8.5
Reflection shellResolution: 2.07→2.12 Å / Num. unique obs: 940 / CC1/2: 0.807 / CC star: 0.945
Serial crystallography sample deliveryMethod: fixed target

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Processing

Software
NameVersionClassification
PHENIX2.0-5936_9999refinement
CrystFELdata reduction
CrystFELdata scaling
PHENIXphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.07→20.6 Å / SU ML: 0.2972 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 23.1958
Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
RfactorNum. reflection% reflection
Rfree0.2342 1486 10 %
Rwork0.2047 13377 -
obs0.2076 14863 99.75 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.1 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso mean: 44.77 Å2
Refinement stepCycle: LAST / Resolution: 2.07→20.6 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1374 0 1 30 1405
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00731408
X-RAY DIFFRACTIONf_angle_d0.77971905
X-RAY DIFFRACTIONf_chiral_restr0.0478221
X-RAY DIFFRACTIONf_plane_restr0.0049245
X-RAY DIFFRACTIONf_dihedral_angle_d16.4389541
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.07-2.140.41320.3481187X-RAY DIFFRACTION100
2.14-2.210.32871300.26271177X-RAY DIFFRACTION99.92
2.21-2.30.3081320.22351194X-RAY DIFFRACTION100
2.3-2.410.26461330.23231201X-RAY DIFFRACTION100
2.41-2.530.29081340.24941194X-RAY DIFFRACTION99.92
2.53-2.690.27611320.22911196X-RAY DIFFRACTION100
2.69-2.90.27521350.2181211X-RAY DIFFRACTION99.93
2.9-3.190.28641360.21171222X-RAY DIFFRACTION100
3.19-3.650.20621370.18291229X-RAY DIFFRACTION100
3.65-4.590.1631390.16531254X-RAY DIFFRACTION99.93
4.59-20.60.22771460.20491312X-RAY DIFFRACTION97.79

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