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1ELV

CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN COMPLEMENT C1S PROTEASE

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsESRF BEAMLINE ID14-4
Synchrotron siteESRF
BeamlineID14-4
Temperature [K]100
Detector technologyCCD
Collection date1998-09-24
DetectorMARRESEARCH
Spacegroup nameP 1 21 1
Unit cell lengths39.080, 79.650, 60.210
Unit cell angles90.00, 91.24, 90.00
Refinement procedure
Resolution15.000 - 1.700
R-factor0.185

*

Rwork0.186
R-free0.21900
RMSD bond length0.020
RMSD bond angle0.024
Data reduction softwareXDS
Data scaling softwareXDS
Refinement softwareREFMAC
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]15.0001.750
High resolution limit [Å]1.7001.700
Rmerge0.037

*

0.247

*

Total number of observations115710

*

Number of reflections39489

*

<I/σ(I)>16.93.4
Completeness [%]93.075.8
Redundancy2.91.5
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1Vapor diffusion

*

7.44

*

PEG 4K 34%, AMMONIUM SULFATE 100mM, pH 7.4, VAPOR DIFFUSION, HANGING DROP, temperature 277K
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropprotein6 (mg/ml)
21dropTEA-HCl50 (mM)
31drop145 (mM)
41reservoirPEG400034 (%)
51reservoirammonium sulfate100 (mM)

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