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1US8

The Rad50 signature motif: essential to ATP binding and biological function

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsSSRL BEAMLINE BL11-1
Synchrotron siteSSRL
BeamlineBL11-1
Temperature [K]294
Collection date2001-11-15
Spacegroup nameP 21 21 21
Unit cell lengths67.541, 67.851, 69.930
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution20.000

*

- 2.100
R-factor0.219
Rwork0.219
R-free0.24900

*

Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)1f2t
RMSD bond length0.005
RMSD bond angle1.080

*

Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwareAMoRE
Refinement softwareCNS (1.1)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]20.000

*

2.140
High resolution limit [Å]2.1002.050
Rmerge0.0570.279
Total number of observations200189

*

Number of reflections25989
<I/σ(I)>103
Completeness [%]99.298.9

*

Redundancy44
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1Vapor diffusion, sitting drop

*

7

*

20 % PEG8000, 0.1 M MES PH 6.0, 0.2 M CALCIUM ACETATE
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropprotein4 (mg/ml)
101reservoircalcium acetate0.2 (M)
21dropTris-HCl20 (mM)pH7.0
31drop200 (mM)
41dropdithiothreitol1 (mM)
51dropEDTA0.5 (mM)
61dropATPgammaS2.5 (mM)
71drop10 (mM)
81reservoirPEG800020 (%(w/v))
91reservoirMES0.1 (M)pH6.0

219869

PDB entries from 2024-05-15

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