1FZG

CRYSTAL STRUCTURE OF FRAGMENT D FROM HUMAN FIBRINOGEN WITH THE PEPTIDE LIGAND GLY-HIS-ARG-PRO-AMIDE

Experimental procedure

Source type	SYNCHROTRON
Source details	NSLS BEAMLINE X12C
Synchrotron site	NSLS
Beamline	X12C
Temperature [K]	297
Detector technology	CCD
Collection date	1998-08
Spacegroup name	P 21 21 21
Unit cell lengths	54.800, 149.400, 234.700
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	30.000 - 2.500
R-factor	0.233
Rwork	0.233
R-free	0.30200
Starting model (for MR)	1fzf
RMSD bond length	0.018
RMSD bond angle	3.400
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	X-PLOR (3.843)
Refinement software	X-PLOR (3.843)

Data quality characteristics

	Overall
Low resolution limit [Å]	30.000
High resolution limit [Å]	2.500
Rmerge	0.111
Total number of observations	737489 *
Number of reflections	66513
Completeness [%]	96.0
Redundancy	11.1

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, sitting drop *	7 *		pH 7.8

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	10 (mg/ml)
2	1	drop	GHRPam	10 (mM)
3	1	reservoir	Tris-HCl	50 (mM)
4	1	reservoir		10 (mM)	or 20mM
5	1	reservoir	PEG3350	12 (%)
6	1	reservoir	sodium azide	2 (mM)