1DFC

CRYSTAL STRUCTURE OF HUMAN FASCIN, AN ACTIN-CROSSLINKING PROTEIN

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU200
Temperature [K]	291
Detector technology	AREA DETECTOR
Collection date	1997-06-19
Detector	SIEMENS
Spacegroup name	C 1 2 1
Unit cell lengths	165.426, 71.689, 116.924
Unit cell angles	90.00, 132.17, 90.00

Refinement procedure

Resolution	25.000 * - 2.900
R-factor	0.184
Rwork	0.184
R-free	0.26800
Structure solution method	MIR
RMSD bond length	0.009 *
RMSD bond angle	1.400 *
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	PHASES (V. 95)
Refinement software	CNS

Data quality characteristics

	Overall
Low resolution limit [Å]	23.030
High resolution limit [Å]	2.900
Rmerge	0.048 *
Number of reflections	21421 *
<I/σ(I)>	19.1
Completeness [%]	94.2 *
Redundancy	2.6

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	8 *	298	PEG 4000, hepes, dtt, sodium azide , pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	20 (mg/ml)
2	1	drop	Tris-HCl	10 (mM)	pH8.0
3	1	drop		10 (mM)
4	1	drop		30 (mM)
5	1	drop	EDTA	0.1 (mM)
6	1	drop	dithiothreitol	1 (mM)
7	1	reservoir	PEG4000	20 (%)
8	1	reservoir	HEPES	0.1 (M)	pH7.5
9	1	reservoir	dithiothreitol	1 (mM)