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1RER

Crystal structure of the homotrimer of fusion glycoprotein E1 from Semliki Forest Virus.

Experimental procedure
Experimental methodMAD
Source typeSYNCHROTRON
Source detailsSLS BEAMLINE X06SA
Synchrotron siteSLS
BeamlineX06SA
Temperature [K]100
Detector technologyCCD
Collection date2003-03-03
DetectorMARRESEARCH
Wavelength(s)1.53596, 1.53646, 1.18080
Spacegroup nameP 31 2 1
Unit cell lengths198.197, 198.197, 116.250
Unit cell angles90.00, 90.00, 120.00
Refinement procedure
Resolution20.000 - 3.200
R-factor0.266
Rwork0.265
R-free0.28500
Structure solution methodMAD, MIR
Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwareSOLVE
Refinement softwareCNS
Data quality characteristics
 Overall
Low resolution limit [Å]20.000
High resolution limit [Å]3.200
Number of reflections40912
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP44

*

PEG 400, NaBr, detergent DDAO, HO3+, VAPOR DIFFUSION, HANGING DROP
1VAPOR DIFFUSION, HANGING DROP44

*

PEG 400, NaBr, detergent DDAO, HO3+, VAPOR DIFFUSION, HANGING DROP
1VAPOR DIFFUSION, HANGING DROP44

*

PEG 400, NaBr, detergent DDAO, HO3+, VAPOR DIFFUSION, HANGING DROP
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11reservoirDDAO15 (mM)
21reservoir250 (mM)
31reservoirTris-HCl25 (mM)
41reservoirPEG40002.5-12.5 (%)pH4.

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PDB entries from 2024-05-15

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