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1IXG

PHOSPHATE-BINDING PROTEIN MUTANT WITH THR 141 REPLACED BY ASP (T141D), COMPLEXED WITH PHOSPATE

Experimental procedure
Source typeSYNCHROTRON
Source detailsSSRL BEAMLINE BL7-1
Synchrotron siteSSRL
BeamlineBL7-1
Temperature [K]100
Detector technologyIMAGE PLATE
Collection date1995-07
Spacegroup nameP 21 21 21
Unit cell lengths41.645, 63.493, 123.788
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution28.100 - 1.050
R-factor0.109
R-free0.13900
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)1pbp
Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwareSHELXL-96
Refinement softwareSHELXL-96
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]28.1001.090
High resolution limit [Å]1.0501.050
Rmerge0.0480.157
Number of reflections111988
<I/σ(I)>29.53.8
Completeness [%]71.732.2
Redundancy7.73.7
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1Vapor diffusion, hanging drop

*

4.5Wang, Z., (1994) J.Biol.Chem., 269, 25091.

*

Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropprotein7.25 (mg/ml)
21droppotassium phosphate1.5 (mM)
31dropPEG600013.5 (%(w/v))
41drop37.5 (mM)
51droppotassium acetate15 (mM)
61reservoirPEG600018 (%(w/v))
71reservoir50 (mM)
81reservoirpotassium phosphate2 (mM)
91reservoirpotassium acetate20 (mM)

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