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1GT9

High resolution crystal structure of a thermostable serine-carboxyl type proteinase, kumamolisin (kscp)

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsMPG/DESY, HAMBURG BEAMLINE BW6
Synchrotron siteMPG/DESY, HAMBURG
BeamlineBW6
Temperature [K]100
Detector technologyCCD
DetectorMARRESEARCH
Spacegroup nameP 1 21 1
Unit cell lengths54.860, 78.250, 73.530
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution19.520 - 1.380
R-factor0.194
Rwork0.194
R-free0.20800
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)1ga1
RMSD bond length0.011
RMSD bond angle1.630
Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwareAMoRE
Refinement softwareCNS (1.2)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]19.5201.410
High resolution limit [Å]1.3801.380
Rmerge0.064

*

0.232
Total number of observations603967

*

Number of reflections120406

*

Completeness [%]95.579
Redundancy4.84.5
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1Vapor diffusion, sitting drop

*

5

*

20

*

100 MM SODIUM ACETATE PH 4.5, 400 MM AMMONIUM SULPHATE
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropprotein9 (mg/ml)
21drop25 (mM)
31dropsodium acetate50 (mM)pH5.
41reservoirammonium sulfate1.2 (M)
51reservoirsodium acetate0.1 (M)pH5.2

217705

PDB entries from 2024-03-27

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