1A98

XPRTASE FROM E. COLI COMPLEXED WITH GMP

Experimental procedure

Source type	ROTATING ANODE
Source details	RIGAKU RUH2R
Temperature [K]	289
Detector technology	IMAGE PLATE
Collection date	1994-03-29
Detector	RIGAKU RAXIS IIC
Spacegroup name	C 1 2 1
Unit cell lengths	84.166, 70.927, 54.051
Unit cell angles	90.00, 113.40, 90.00

Refinement procedure

Resolution	50.000 - 2.250
R-factor	0.21
Rwork	0.210
R-free	0.22400
Structure solution method	MOLECULAR REPLACEMENT MOLECULAR REPLACEMENT
Starting model (for MR)	1nul
RMSD bond length	0.005
RMSD bond angle	1.075 *
Data reduction software	PROCESS ((HIGASHI))
Data scaling software	PROCESS ((HIGASHI))
Phasing software	X-PLOR (3.851)
Refinement software	X-PLOR (3.851)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000 *	2.330
High resolution limit [Å]	2.250	2.250
Rmerge	0.037	0.172
Total number of observations	16902 *
Number of reflections	11089
<I/σ(I)>	11.8	3.4
Completeness [%]	79.5	66.9
Redundancy	1.5	1.4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	7.6 *		XPRT WAS CRYSTALLIZED FROM 20% PEG4000 IN 0.1 M TRIS-HCL, pH 8.0

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	PEG4000	20 (%)
2	1	reservoir	Tris-HCl	0.1 (M)	pH8.0
3	1	drop	protein	20 (mg/ml)
4	1	drop	Tris-HCl	50 (mM)	pH7.6
5	1	drop		10 (mM)