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1A1A

C-SRC (SH2 DOMAIN WITH C188A MUTATION) COMPLEXED WITH ACE-FORMYL PHOSPHOTYR-GLU-(N,N-DIPENTYL AMINE)

Experimental procedure
Source typeROTATING ANODE
Source detailsSIEMENS
Temperature [K]103
Detector technologyIMAGE PLATE
Collection date1994-09
DetectorRIGAKU RAXIS IIC
Spacegroup nameP 21 21 21
Unit cell lengths51.400, 65.400, 74.600
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution6.000 - 2.000
R-factor0.198
Rwork0.198
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)1shd
RMSD bond length0.017
RMSD bond angle23.060

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Data reduction softwareR-AXIS
Data scaling softwareR-AXIS
Phasing softwareX-PLOR
Refinement softwareX-PLOR
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]50.0002.250
High resolution limit [Å]2.0002.000
Rmerge0.0640.132
Number of reflections18250
<I/σ(I)>21.685.5
Completeness [%]94.890
Redundancy2.72.99
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1Vapor diffusion, hanging drop

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84

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PROTEIN WAS CRYSTALLIZED FROM 1.0 M LI2SO4, 2% PEG8000 AT 4C. THE CRYSTAL WAS SOAKED IN 25% GLYCEROL PRIOR TO DATA COLLECTION., pH 8.0, temperature 277K
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropprotein125 (mg/ml)
21dropHEPES20 (mM)
31drop350 (mM)
41dropdithiothreitol5 (mM)
51dropEDTA5 (mM)
61reservoir1.0 (M)
71reservoirPEG80002 (%)

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