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1UIX

Coiled-coil structure of the RhoA-binding domain in Rho-kinase

Experimental procedure
Experimental methodMAD
Source typeSYNCHROTRON
Source detailsPHOTON FACTORY BEAMLINE BL-18B
Synchrotron sitePhoton Factory
BeamlineBL-18B
Temperature [K]93
Detector technologyDIFFRACTOMETER
Collection date1999-12-15
DetectorWEISSENBERG
Wavelength(s)0.9784, 0.9778, 0.9600, 1.000
Spacegroup nameC 1 2 1
Unit cell lengths148.000, 26.100, 39.600
Unit cell angles90.00, 90.40, 90.00
Refinement procedure
Resolution39.500 - 1.800
R-factor0.219
Rwork0.193
R-free0.23600
Structure solution methodMAD
RMSD bond length0.018

*

RMSD bond angle1.511

*

Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwareSHARP
Refinement softwareREFMAC (5.1.24)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]39.5301.860
High resolution limit [Å]1.8001.800
Rmerge0.0450.082
Total number of observations139215

*

Number of reflections12896
<I/σ(I)>18.214.8
Completeness [%]89.068.4
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP7277Thara, K., (2000) Acta Crystallogr., D56, 1042.

*

Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropprotein2.7 (mg/ml)
21dropHEPES55 (mM)pH7.0
31drop23 (mM)
41dropPEG100011 (%)
51dropethylene glycol14 (%)
61dropn-octanoylsucrose22 (mM)
71reservoirHEPES100 (mM)pH7.0
81reservoirPEG100025 (%)
91reservoirethylene glycol30 (%)

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