1A97

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	1996-04-11
Detector	RIGAKU RAXIS IIC
Spacegroup name	P 43 21 2
Unit cell lengths	94.042, 94.042, 166.914
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	50.000 - 2.600
R-factor	0.233
Rwork	0.233
R-free	0.26300
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1nul
RMSD bond length	0.004
RMSD bond angle	24.900 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	X-PLOR (3.851)
Refinement software	X-PLOR (3.851)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	100.000	2.590
High resolution limit [Å]	2.600	2.500
Rmerge	0.073	0.282
Total number of observations	76094 *
Number of reflections	23936
<I/σ(I)>	11.1	2.6
Completeness [%]	89.5	81.1
Redundancy	3.2	2.1

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	7.6 *		XPRT WAS CRYSTALLISED FROM 15 - 20% PEG 4000, 0.1 M AMMONIUM PHOSPHATE IN 0.1 M BORATE, PH 9., pH 9.0

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	PEG4000	15-20 (%(w/v))
2	1	reservoir	borate	0.1 (M)
3	1	reservoir	ammonium phosphate	0.2 (M)
4	1	drop	protein	20 (mg/ml)
5	1	drop	Tris-HCl	50 (mM)	pH7.6
6	1	drop		10 (mM)