1RF1

Crystal Structure of Fragment D of gammaE132A Fibrinogen with the Peptide Ligand Gly-His-Arg-Pro-amide

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SSRL BEAMLINE BL9-1
Synchrotron site	SSRL
Beamline	BL9-1
Temperature [K]	100
Detector technology	CCD
Collection date	2003-01-12
Detector	ADSC QUANTUM 315
Wavelength(s)	0.98396
Spacegroup name	P 21 21 21
Unit cell lengths	89.714, 94.683, 228.198
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	18.000 * - 2.530
R-factor	0.234
Rwork	0.234
R-free	0.28100
Structure solution method	rigid body refinement
Starting model (for MR)	1ltj
RMSD bond length	0.006
RMSD bond angle	1.240 *
Data reduction software	HKL-2000
Data scaling software	SCALEPACK
Phasing software	CNS
Refinement software	CNS (1.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	18.000	2.620
High resolution limit [Å]	2.530	2.530
Rmerge	0.090 *	0.359 *
Total number of observations	264892 *
Number of reflections	66025
<I/σ(I)>	13.8	4
Completeness [%]	99.9	100
Redundancy	4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.4 *	4 *	9-10% PEG 3350, 12.5 mM calcium chloride, 2 mM sodium azide, 50 mM Tris pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	10 (mg/ml)
2	1	drop	Tris	50 (mM)	pH7.4
3	1	drop	GHRPam	2 (mM)
4	1	reservoir	Tris	50 (mM)	pH8.5
5	1	reservoir		2 (mM)
6	1	reservoir		12.5 (mM)
7	1	reservoir	PEG3350	9-10 (%)