1BGX

TAQ POLYMERASE IN COMPLEX WITH TP7, AN INHIBITORY FAB

Experimental procedure

Source type	ROTATING ANODE
Source details	SIEMENS
Temperature [K]	298
Detector technology	AREA DETECTOR
Collection date	1997-10
Detector	SIEMENS
Spacegroup name	P 1
Unit cell lengths	76.600, 89.100, 89.300
Unit cell angles	100.70, 115.30, 95.30

Refinement procedure

Resolution	8.000 - 2.300
R-factor	0.189
Rwork	0.189
R-free	0.25300
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1AYL AND 1TAQ
RMSD bond length	0.010
RMSD bond angle	19.100 *
Data reduction software	XDS
Data scaling software	XDS
Phasing software	X-PLOR (3.8)
Refinement software	X-PLOR (3.8)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	27.700	2.500
High resolution limit [Å]	2.300	2.300
Rmerge	0.074	0.122
Total number of observations	414722 *
Number of reflections	81111
<I/σ(I)>	8.2	8
Completeness [%]	82.0	75.9
Redundancy	5.1	3.8

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.4	20 *	PROTEIN WAS CRYSTALLIZED FROM 22% PEG 3350, 200 MM TRIS/HCL, PH 7.4. COMPLEX WAS MADE AT A PROTEIN CONCENTRATION OF 0.5 MG/ML, LEFT FOR 2-3 DAYS AT 4 DEGREES CELSIUS, CONCENTRATED TO 5MG/ML PROTEIN AND CRYSTALLIZATION CARRIED OUT IN HANGING DROPS., vapor diffusion - hanging drop, temperature 277K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	5 (mg/ml)
2	1	reservoir	PEG3350	22 (%)
3	1	reservoir	Tris-HCl	200 (mM)	pH7.4
4	1	reservoir		0.1 (%)