1GTG

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

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU200
Temperature [K]	100
Detector technology	IMAGE PLATE
Detector	MARRESEARCH
Wavelength(s)	1.5418
Spacegroup name	P 1 21 1
Unit cell lengths	42.630, 78.320, 49.000
Unit cell angles	90.00, 106.33, 90.00

Refinement procedure

Resolution	36.300 * - 2.270 *
R-factor	0.206 *
Rwork	0.206
R-free	0.25800 *
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1ga1
RMSD bond length	0.010
RMSD bond angle	1.650
Data reduction software	MOSFLM
Data scaling software	SCALA
Phasing software	AMoRE
Refinement software	CNS (1.2)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	36.300 *	2.390
High resolution limit [Å]	2.270 *	2.270
Rmerge	0.091 *	0.232
Total number of observations	26014 *
Number of reflections	13692 *
<I/σ(I)>	7	3.1
Completeness [%]	95.6	87.4 *
Redundancy	1.9	1.8

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, sitting drop *	5 *	20 *	100 MM SODIUM ACETATE PH 5.2 1.2 M 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