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1AY2

STRUCTURE OF THE FIBER-FORMING PROTEIN PILIN AT 2.6 ANGSTROMS RESOLUTION

Experimental procedure
Source typeSYNCHROTRON
Source detailsSSRL BEAMLINE BL7-1
Synchrotron siteSSRL
BeamlineBL7-1
Temperature [K]290
Detector technologyIMAGE PLATE
Collection date1993-05
DetectorMARRESEARCH
Spacegroup nameC 2 2 2
Unit cell lengths127.580, 121.080, 26.860
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution10.000 - 2.600
R-factor0.194
Rwork0.194
Structure solution methodMIR
RMSD bond length0.017
RMSD bond angle1.359

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Data reduction softwareMOSFLM
Data scaling softwareCCP4 ((AGROVATA)
Phasing softwareX-PLOR (3.1)
Refinement softwareX-PLOR (3.1)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]24.0002.780
High resolution limit [Å]2.6002.600
Rmerge0.081

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Number of reflections6494
<I/σ(I)>6.72.3
Completeness [%]95.080.2
Redundancy44.2
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1Vapor diffusion, hanging drop

*

8Parge, H.E., (1990) J. Biol. Chem., 265, 2278.

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Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropprotein1 (%(w/v))
101reservoir0.02 (%)
21dropBOG1-1.5 (%)
31dropTris-HCl100 (mM)
41drop20 (mM)
51dropdithiothreitol1 (mM)
61drop0.02 (%)
71dropPEG40036-45 (%)
81reservoirTris-HCl100 (mM)
91dropreservoir

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数据于2024-03-27公开中

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