4HWU

Crystal structure of the Ig-C2 type 1 domain from mouse Fibroblast growth factor receptor 2 (FGFR2) [NYSGRC-005912]

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	NSLS BEAMLINE X29A
Synchrotron site	NSLS
Beamline	X29A
Temperature [K]	100
Detector technology	CCD
Collection date	2012-10-11
Detector	ADSC QUANTUM 315
Wavelength(s)	1.5498
Spacegroup name	P 31 2 1
Unit cell lengths	53.818, 53.818, 122.817
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	46.608 - 2.903
R-factor	0.2277
Rwork	0.227
R-free	0.25220
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.011
RMSD bond angle	1.405
Data scaling software	SCALEPACK
Phasing software	PHASER
Refinement software	PHENIX (1.8.1_1168)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000	50.000	2.950
High resolution limit [Å]	2.900	7.860	2.900
Rmerge	0.178	0.057
Number of reflections	8822
<I/σ(I)>	17.75
Completeness [%]	100.0	100	100
Redundancy	11.1	11.3	9.1

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION	7	298	Protein (20 mM Hepes, pH 7.5, 150 mM NaCl, 10% glycerol; Reservoir (1.1M Malonic acid, 0.15M Ammonium Citrate Tribasic, 0.072M Succinic acid, 0.18M DL-Malic Acid, 0.24M Sodium acetate, 0.3M Sodium formate, 0.096M Ammonium tartrate dibasic, pH 7.0), Cryoprotection (Reservoir + 20% Glycerol, a speck of I3C (Jena Biosciences) heavy atom), Sitting Drop Vapor Diffusion, temperature 298K, VAPOR DIFFUSION