1JJO

Crystal Structure of Mouse Neuroserpin (Cleaved form)

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	ENRAF-NONIUS FR571
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	1999-07-06
Detector	MARRESEARCH
Wavelength(s)	1.5418
Spacegroup name	P 1 21 1
Unit cell lengths	64.290, 108.690, 45.990
Unit cell angles	90.00, 101.28, 90.00

Refinement procedure

Resolution	16.890 - 3.060
R-factor	0.232 *
Rwork	0.232
R-free	0.30800
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	homology model based on all available cleaved serpin structures
RMSD bond length	0.008
RMSD bond angle	1.419
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	CNS (0.9)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	17.000 *	3.100
High resolution limit [Å]	3.060	3.060
Rmerge	0.155 *	0.422 *
Number of reflections	9419	7975 *
<I/σ(I)>	7	2
Completeness [%]	79.7	74.6 *
Redundancy	2.57	2.3

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	6.1	20 *	25% PEG8000, 0.2M H2PO4(NH4), 0.1M Tris-HCl, pH 6.1, VAPOR DIFFUSION, SITTING DROP, temperature 293K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	25 (mg/ml)
2	1	reservoir	PEG8000	25 (%)
3	1	reservoir		0.2 (M)
4	1	reservoir	Tris-HCl	0.1 (M)	pH6.1