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1O0E

1.9 Angstrom Crystal Structure of a plant cysteine protease Ervatamin C

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeROTATING ANODE
Source detailsRIGAKU RU200B
Temperature [K]293
Detector technologyIMAGE PLATE
Collection date1999-01-04
DetectorMARRESEARCH
Wavelength(s)1.5418
Spacegroup nameP 21 21 21
Unit cell lengths43.729, 82.691, 133.048
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution15.000

*

- 1.900
R-factor0.177
Rwork0.177
R-free0.19000
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)1iwd
RMSD bond length0.006
RMSD bond angle24.000

*

Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwareAMoRE
Refinement softwareCNS (1.0)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]15.0001.940
High resolution limit [Å]1.9001.900
Rmerge0.0600.560
Total number of observations157915

*

Number of reflections38978
<I/σ(I)>20.152.86
Completeness [%]97.999.8
Redundancy4.05
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP7293PEG8000, potassium phosphate monobasic, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropprotein13 (mg/ml)
21dropsodium phosphate0.01 (M)pH7.0
31reservoirpotassium dihydrogen orhtophosphate0.05 (M)
41reservoirPEG800020 (%(w/v))

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