3BIF

6-PHOSPHOFRUCTO-2-KINASE/FRUCTOSE-2,6-BISPHOSPHATASE EMPTY 6-PF-2K ACTIVE SITE

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU200
Temperature [K]	120
Detector technology	IMAGE PLATE
Collection date	1997-10-09
Detector	MACSCIENCE
Spacegroup name	C 1 2 1
Unit cell lengths	106.700, 108.700, 71.700
Unit cell angles	90.00, 129.50, 90.00

Refinement procedure

Resolution	30.000 - 2.300
R-factor	0.197 *
Rwork	0.197
R-free	0.24300
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1bif
RMSD bond length	0.008
RMSD bond angle	21.600 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	X-PLOR
Refinement software	X-PLOR (3.851)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	2.350
High resolution limit [Å]	2.300	2.300
Rmerge	0.039 *
Number of reflections	23883
<I/σ(I)>	36.5	7.16
Completeness [%]	88.1	84.9
Redundancy	2.64	2.3

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	7.5 *	4 *	PROTEIN WAS CRYSTALLIZED FROM 50MM SUCCINATE, PH 5.5, 50MM TRIS-PO4, PH 7.5, 11% PEG 4000, 100UM EDTA, 10MM DTT, 10% GLYCEROL, 3MM MGCL2., pH 7.0

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	RT2K-Wo	10 (mg/ml)
10	1	reservoir	succinate	50 (mM)
11	1	reservoir	Tris-PO4	50 (mM)
12	1	reservoir	EDTA	0.100 (mM)
13	1	reservoir	dithiothreitol	10 (mM)
14	1	reservoir	glycerol	10 (%)
15	1	reservoir		3 (mM)
2	1	drop	Tris-PO4	50 (mM)
3	1	drop	glycerol	5 (%)
4	1	drop	EDTA	0.100 (mM)
5	1	drop	dithiothreitol	10 (mM)
6	1	drop	octyl beta-D-glucopyranoside	0.5 (%)
7	1	drop	F6P	3 (mM)
8	1	drop	AMP-PNP	1 (mM)
9	1	reservoir	PEG4000	11 (%)