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1B27

STRUCTURAL RESPONSE TO MUTATION AT A PROTEIN-PROTEIN INTERFACE

Replaces:  1BV0
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 lengths202.917, 43.319, 83.177
Unit cell angles90.00, 110.50, 90.00
Refinement procedure
Resolution24.000 - 2.100
R-factor0.195

*

Rwork0.195
R-free0.25900
Structure solution methodOTHER
Starting model (for MR)1brs
RMSD bond length0.009
RMSD bond angle0.027
Data reduction softwareMOSFLM
Data scaling softwareCCP4 ((SCALA))
Phasing softwareX-PLOR
Refinement softwareREFMAC
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]24.1102.130
High resolution limit [Å]2.0802.080
Rmerge0.0660.357

*

Number of reflections32841
<I/σ(I)>10.43.32
Completeness [%]79.865.4
Redundancy2.42
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1Vapor diffusion, hanging drop

*

818-24% PEG-8K 0.2 M AMMONIUM SULPHATE 0.1 M TRIS PH8.0
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11reservoirPEG800018-24 (%(w/v))
21reservoirammonium sulfate0.2 (M)
31reservoirTris0.1 (M)
41dropprotein20 (mg/ml)

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PDB entries from 2024-05-15

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