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1MBM

NSP4 proteinase from Equine Arteritis Virus

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeROTATING ANODE
Source detailsRIGAKU RU300
Temperature [K]105
Detector technologyIMAGE PLATE
Collection date2001-09-20
DetectorRIGAKU RAXIS IV
Wavelength(s)1.5418
Spacegroup nameP 1
Unit cell lengths56.612, 60.326, 62.637
Unit cell angles74.08, 63.30, 66.18
Refinement procedure
Resolution16.200

*

- 2.000
R-factor0.20726
Rwork0.204
R-free0.26100

*

Structure solution methodMIR
RMSD bond length0.007
RMSD bond angle1.271
Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwareSOLVE
Refinement softwareREFMAC (5.0)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]16.200

*

2.070
High resolution limit [Å]2.0002.000
Rmerge0.0500.179
Total number of observations169296

*

Number of reflections431714151

*

<I/σ(I)>22.46.1
Completeness [%]95.091.5
Redundancy3.93.7
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP8.5

*

PEG 8000, sodium cirate, ethylene glycol, sodium malonate, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 105K
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropprotein25 (mg/ml)
21reservoirPEG2000 MME23 (%(w/v))
31reservoirTris100 (mM)pH8.5
41reservoirethylene glycol100 (%(w/v))
51reservoirammonium acetate0.2 (M)

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