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1B2U

STRUCTURAL RESPONSE TO MUTATION AT A PROTEIN-PROTEIN INTERFACE

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeROTATING ANODE
Source detailsELLIOTT GX-13
Temperature [K]100
Detector technologyIMAGE PLATE
Collection date1996-01
DetectorMARRESEARCH
Spacegroup nameC 1 2 1
Unit cell lengths201.230, 43.020, 83.470
Unit cell angles90.00, 110.70, 90.00
Refinement procedure
Resolution21.300 - 2.100
R-factor0.214

*

Rwork0.214
R-free0.27600
Structure solution methodOTHER
Starting model (for MR)1brs
RMSD bond length0.014
RMSD bond angle0.032
Data reduction softwareMOSFLM
Data scaling softwareCCP4 ((SCALA))
Phasing softwareX-PLOR
Refinement softwareREFMAC
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]22.3002.150
High resolution limit [Å]2.1002.100
Rmerge0.065

*

0.298
Number of reflections32841
<I/σ(I)>14.454
Completeness [%]98.999.7

*

Redundancy3.63
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1Vapor diffusion, hanging drop

*

6.521% PEG-8K 0.2 M AMMONIUM SULPHATE 0.1 M NA CACODYLATE PH6.5
Crystallization Reagents
IDcrystal IDsolution IDreagent nameconcentrationdetails
111PEG 8000
211NA CACODYLATE
311NH4 SULFATE
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropprotein20 (mg/ml)
21reservoirPEG800018-24 (%(w/v))
31reservoirsodium cacodylate0.1 (M)

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