2HOD

Crystal Structure of Fragment D from Human Fibrinogen Complexed with Gly-hydroxyPro-Arg-Pro-amide

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ALS BEAMLINE 8.2.2
Synchrotron site	ALS
Beamline	8.2.2
Temperature [K]	100
Detector technology	CCD
Collection date	2005-03-04
Detector	ADSC QUANTUM 315
Wavelength(s)	0.95
Spacegroup name	P 1 2 1
Unit cell lengths	81.647, 47.069, 431.460
Unit cell angles	90.00, 90.06, 90.00

Refinement procedure

Resolution	30.000 - 2.900
R-factor	0.2384
Rwork	0.268
R-free	0.34710
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1fzg
RMSD bond length	0.009
RMSD bond angle	1.606
Data reduction software	HKL-2000
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	CNS (1.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	2.900
High resolution limit [Å]	2.800	2.800
Number of reflections	71011
Completeness [%]	85.3	42
Redundancy	3.2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.5	295	equal volumes of 10 mg/ml fragment D, 5 mM Gly-hydroxyPro-Arg-Pro-amide, 50 mM Tris, pH 7.0 and 16% PEG 3350, 50 mM Tris pH 8.0 mM 20 mM CaCl2, 2 mM sodium azide., pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 295K