2OYH

Crystal Structure of Fragment D of gammaD298,301A Fibrinogen with the Peptide Ligand Gly-His-Arg-Pro-Amide

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 22-ID
Synchrotron site	APS
Beamline	22-ID
Temperature [K]	100
Detector technology	CCD
Collection date	2003-06-14
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	1.00
Spacegroup name	P 21 21 21
Unit cell lengths	89.164, 94.119, 226.730
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	18.000 - 2.400
R-factor	0.22
Rwork	0.220
R-free	0.25900
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1ltj
RMSD bond length	0.006
RMSD bond angle	1.200
Data reduction software	HKL-2000
Data scaling software	HKL-2000
Phasing software	CNS
Refinement software	CNS (1.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	2.490
High resolution limit [Å]	2.400	2.400
Number of reflections	71647	5983
<I/σ(I)>	15.4	1.9
Completeness [%]	96.0	81.6
Redundancy	5.7	4.8

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8.5	277	5 microL of 10 mg/mL protein in HBS with 3 mM GHRP were mixed with an identical volume of well solution containing 50 mM Tris, pH 8.5, 2 mM NaN3, 12.5 mM CaCl2, and 11% PEG 3350, VAPOR DIFFUSION, SITTING DROP, temperature 277K