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1AM1

ATP BINDING SITE IN THE HSP90 MOLECULAR CHAPERONE

Experimental procedure
Source typeSYNCHROTRON
Source detailsSRS BEAMLINE PX9.5
Synchrotron siteSRS
BeamlinePX9.5
Temperature [K]110
Detector technologyIMAGE PLATE
Collection date1997-06
DetectorMARRESEARCH
Spacegroup nameP 43 2 2
Unit cell lengths73.910, 73.910, 110.970
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution8.000 - 2.000
R-factor0.189
Rwork0.189
Structure solution methodISOMORPHOUS REPLACEMENT
Starting model (for MR)1ah6
RMSD bond length0.006
RMSD bond angle25.700

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Data reduction softwareMOSFLM
Data scaling softwareCCP4 ((AGROVATA)
Phasing softwareX-PLOR (3.851)
Refinement softwareX-PLOR (3.851)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]24.0002.050
High resolution limit [Å]2.0002.000
Rmerge0.116

*

0.240

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Number of reflections21414
<I/σ(I)>3.33
Completeness [%]99.9100
Redundancy3.53.5
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1unknown

*

5PROTEIN WAS CRYSTALLIZED UNDER OIL IN TERASAKI PLATES. THE DROPS CONTAINED 27MG/ML PROTEIN, 9.75%(W/V) PEGME 550, 65MM AMMONIUM SULFATE, 32.5MM SODIUM SUCCINATE PH5.0, 5MM ATP AND 5MM MAGNESIUM CHLORIDE., under oil
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
111protein36 (mg/ml)
211mPEG5503 (%)
31120 (mM)
411Tris-HCl10 (mM)
511nucleotide5 (mM)
6115 (mM)

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PDB entries from 2024-05-15

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