1GT9

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

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	MPG/DESY, HAMBURG BEAMLINE BW6
Synchrotron site	MPG/DESY, HAMBURG
Beamline	BW6
Temperature [K]	100
Detector technology	CCD
Detector	MARRESEARCH
Spacegroup name	P 1 21 1
Unit cell lengths	54.860, 78.250, 73.530
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	19.520 - 1.380
R-factor	0.194
Rwork	0.194
R-free	0.20800
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1ga1
RMSD bond length	0.011
RMSD bond angle	1.630
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	CNS (1.2)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	19.520	1.410
High resolution limit [Å]	1.380	1.380
Rmerge	0.064 *	0.232
Total number of observations	603967 *
Number of reflections	120406 *
Completeness [%]	95.5	79
Redundancy	4.8	4.5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, sitting drop *	5 *	20 *	100 MM SODIUM ACETATE PH 4.5, 400 MM AMMONIUM SULPHATE

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	9 (mg/ml)
2	1	drop		25 (mM)
3	1	drop	sodium acetate	50 (mM)	pH5.
4	1	reservoir	ammonium sulfate	1.2 (M)
5	1	reservoir	sodium acetate	0.1 (M)	pH5.2