1AB4

59KDA FRAGMENT OF GYRASE A FROM E. COLI

Experimental procedure

Source type	ROTATING ANODE
Source details	RIGAKU RUH2R
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	1996-04
Detector	RIGAKU
Spacegroup name	I 41
Unit cell lengths	119.630, 119.630, 94.980
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	15.000 - 2.800
R-factor	0.226
Rwork	0.226
R-free	0.31000
Structure solution method	MIR
RMSD bond length	0.006
RMSD bond angle	22.400 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	X-PLOR (3.843)
Refinement software	X-PLOR (3.843)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	15.000	2.900
High resolution limit [Å]	2.800	2.800
Rmerge	0.047 *
Number of reflections	16475
<I/σ(I)>	20	10
Completeness [%]	100.0	100
Redundancy	7	6

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	unknown *	8.5	4 *	PROTEIN WAS CRYSTALLISED FROM 8% PEG 8000, 0.02M NACL 0.1 M TRIS PH8.5.

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	1	PEG8000	8 (%)
2	1	1		20 (mM)
3	1	1	Tris-HCl	0.1 (M)