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1GTG

Crystal structure of the thermostable serine-carboxyl type proteinase, kumamolysin (kscp)

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeROTATING ANODE
Source detailsRIGAKU RU200
Temperature [K]100
Detector technologyIMAGE PLATE
DetectorMARRESEARCH
Wavelength(s)1.5418
Spacegroup nameP 1 21 1
Unit cell lengths42.630, 78.320, 49.000
Unit cell angles90.00, 106.33, 90.00
Refinement procedure
Resolution36.300

*

- 2.270

*

R-factor0.206

*

Rwork0.206
R-free0.25800

*

Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)1ga1
RMSD bond length0.010
RMSD bond angle1.650
Data reduction softwareMOSFLM
Data scaling softwareSCALA
Phasing softwareAMoRE
Refinement softwareCNS (1.2)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]36.300

*

2.390
High resolution limit [Å]2.270

*

2.270
Rmerge0.091

*

0.232
Total number of observations26014

*

Number of reflections13692

*

<I/σ(I)>73.1
Completeness [%]95.687.4

*

Redundancy1.91.8
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1Vapor diffusion, sitting drop

*

5

*

20

*

100 MM SODIUM ACETATE PH 5.2 1.2 M 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

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PDB entries from 2024-11-06

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