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1HA1

HNRNP A1 (RBD1,2) FROM HOMO SAPIENS

Experimental procedure
Source typeSYNCHROTRON
Source detailsNSLS BEAMLINE X12C
Synchrotron siteNSLS
BeamlineX12C
Temperature [K]100
Detector technologyIMAGE PLATE AREA DETECTOR
Collection date1996-06
DetectorMARRESEARCH
Spacegroup nameP 1 21 1
Unit cell lengths37.600, 43.500, 55.500
Unit cell angles90.00, 94.70, 90.00
Refinement procedure
Resolution8.000 - 1.750
R-factor0.198
Rwork0.198
R-free0.27500
Structure solution methodMIR
RMSD bond length0.015
RMSD bond angle26.500

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Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwareX-PLOR (3.843)
Refinement softwareX-PLOR (3.843)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]50.0001.770
High resolution limit [Å]1.7401.740
Rmerge0.0450.223
Total number of observations42714

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Number of reflections18507
<I/σ(I)>4.34.1
Completeness [%]97.166.2
Redundancy2.31.1
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1Vapor diffusion, hanging drop

*

8.112

*

PROTEIN WAS CRYSTALLIZED FROM 30% PEG 1500, 50 MM NACL, 20 MM TRIS 8.1, THEN MOVED TO 15% ETHYLENE GLYCOL FOR FREEZING.
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropRBD1,218 (mg/ml)
21drop50 (mM)
31dropTris30 (mM)
41dropPEG150014-16 (%)
51reservoir50 (mM)
61reservoirTris50 (mM)
71reservoirPEG150028-32 (%)

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