1LDF

CRYSTAL STRUCTURE OF THE E. COLI GLYCEROL FACILITATOR (GLPF) MUTATION W48F, F200T

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ALS BEAMLINE 5.0.1
Synchrotron site	ALS
Beamline	5.0.1
Temperature [K]	100
Detector technology	CCD
Collection date	2001-11-10
Detector	ADSC
Spacegroup name	I 4 2 2
Unit cell lengths	96.925, 96.925, 185.433
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	35.000 - 2.100
R-factor	0.23 *
Rwork	0.230
R-free	0.24300
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1fx8
RMSD bond length	0.006
RMSD bond angle	1.170
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	CNS
Refinement software	CNS

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	35.000	2.180
High resolution limit [Å]	2.100	2.100
Rmerge	0.085	0.363
Total number of observations	128187 *
Number of reflections	25710
<I/σ(I)>	16
Completeness [%]	97.9	89.6
Redundancy	4.786

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	unknown *	8.9 *	298	GLPF AT 15-20 MG/ML, 28% (W/V) PEG 2000, 100 MM BICINE pH 9.5, 15 % (V/V) GLYCEROL, 35 MM, N-OCTYL-BETA-D-GLUCOSIDE, MGCL2, 5 MM DTT, pH 9.50, VAPOR DIFFUSION, HANGING DROP, temperature 298K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	1	protein	15-20 (mg/ml)
2	1	2	PEG2000	28 (%(w/v))
3	1	2	bicine	100 (mM)
4	1	2	glycerol	15 (%(v/v))
5	1	2	n-octyl-beta-D-glucoside	35 (mM)
6	1	2		300 (mM)
7	1	2	dithiothreitol	5 (mM)