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2C4M

Starch phosphorylase: structural studies explain oxyanion-dependent kinetic stability and regulatory control.

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsESRF BEAMLINE ID14-1
Synchrotron siteESRF
BeamlineID14-1
Temperature [K]100
Detector technologyCCD
Collection date2003-03-16
DetectorADSC CCD
Spacegroup nameP 1 21 1
Unit cell lengths99.266, 187.620, 129.315
Unit cell angles90.00, 112.48, 90.00
Refinement procedure
Resolution30.000 - 1.900
R-factor0.216
Rwork0.216
R-free0.23200
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)1gpa
RMSD bond length0.011
RMSD bond angle1.500
Data reduction softwareMOSFLM
Data scaling softwareSCALA
Phasing softwareMOLREP
Refinement softwareCNS (1.1)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]30.0002.000
High resolution limit [Å]1.9001.900
Rmerge0.0800.240
Number of reflections306185
<I/σ(I)>5.13.1
Completeness [%]89.775.9
Redundancy2.62
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP5HANGING DROP VAPOUR DIFFUSION 8.4MG/ML PROTEIN SOLUTION, 0.1M SODIUM ACETATE PH 5.0, 8% PEG 8,000, 0.2M SODIUM FORMATE

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