1FZD

STRUCTURE OF RECOMBINANT ALPHAEC DOMAIN FROM HUMAN FIBRINOGEN-420

Experimental procedure

Source type	SYNCHROTRON
Source details	NSLS BEAMLINE X12C
Synchrotron site	NSLS
Beamline	X12C
Temperature [K]	293
Detector technology	CCD
Collection date	1998-02-20
Spacegroup name	P 1
Unit cell lengths	71.250, 105.180, 71.140
Unit cell angles	104.60, 108.95, 71.47

Refinement procedure

Resolution	20.000 - 2.100
R-factor	0.199
Rwork	0.195
R-free	0.25500
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1FCZ (GAMMA DOMAIN)
RMSD bond length	0.013
RMSD bond angle	3.000
Data scaling software	SCALEPACK
Phasing software	X-PLOR
Refinement software	REFMAC

Data quality characteristics

	Overall
Low resolution limit [Å]	20.000
High resolution limit [Å]	2.100
Rmerge	0.098
Total number of observations	1169328 *
Number of reflections	110459
Completeness [%]	91.2
Redundancy	5.2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.5 *		PROTEIN WAS CRYSTALLIZED BY SITTING DROP VAPOUR DIFFUSION FROM 20% PEG 3350, 0.15 M CACL2, 0.1M IMIDAZOLE- ACETATE PH 5.5 0.002 M SODIUM AZIDE, vapor diffusion - sitting drop

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	PEG3350	20 (%)
2	1	reservoir		0.15 (M)
3	1	reservoir	imidazole acetate	0.1 (M)
4	1	reservoir	sodium azide	0.002 (M)
5	1	drop	protain	8 (mg/ml)
6	1	drop	Tris	0.02 (M)