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1NZI

Crystal Structure of the CUB1-EGF Interaction Domain of Complement Protease C1s

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsESRF BEAMLINE ID14-2
Synchrotron siteESRF
BeamlineID14-2
Temperature [K]100
Detector technologyCCD
Collection date2000-04-21
DetectorMARRESEARCH
Wavelength(s)0.933
Spacegroup nameP 1
Unit cell lengths35.134, 47.499, 56.679
Unit cell angles87.74, 78.04, 75.67
Refinement procedure
Resolution30.000 - 1.500
R-factor0.2173
Rwork0.216
R-free0.24600

*

Structure solution methodSAD, MR
Data reduction softwareMOSFLM
Data scaling softwareSCALA
Phasing softwareCNS
Refinement softwareCNS
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]30.0001.580
High resolution limit [Å]1.5001.500
Rmerge0.064

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0.143

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Total number of observations181271

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Number of reflections52518

*

7588

*

<I/σ(I)>6.9
Completeness [%]94.493.3
Redundancy3.5

*

2.2

*

Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP7.4

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20

*

PEG 4000, magnesium chloride, glycerol, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropprotein6.0-7.8 (mg/ml)
21drop145 (mM)
31drop1 (mM)
41dropTEA-HCl50 (mM)pH7.4
51reservoirPEG40030 (%(v/v))
61reservoir0.2 (M)
71reservoirHEPES0.1 (M)pH7.5

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PDB entries from 2024-09-18

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