2IGD

ANISOTROPIC STRUCTURE OF PROTEIN G IGG-BINDING DOMAIN III AT 1.1 ANGSTROM RESOLUTION

Experimental procedure

Source type	SYNCHROTRON
Source details	EMBL/DESY, HAMBURG BEAMLINE X31
Synchrotron site	EMBL/DESY, HAMBURG
Beamline	X31
Temperature [K]	300
Detector technology	IMAGE PLATE
Collection date	1992-04
Detector	MARRESEARCH
Spacegroup name	P 21 21 21
Unit cell lengths	35.050, 40.500, 42.370
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	10.000 - 1.100
R-factor	0.097
R-free	0.12500
Structure solution method	INITIAL MODEL WAS PREVIOUSLY OBTAINED STRUCTURE
Starting model (for MR)	1igd
RMSD bond length	0.020
RMSD bond angle	0.028
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	SHELXL-96
Refinement software	SHELXL-96

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	10.100	1.120
High resolution limit [Å]	1.100	1.100
Rmerge	0.037	0.104
Number of reflections	24145
<I/σ(I)>	39	12
Completeness [%]	97.9	98.1
Redundancy	4.8	3.6

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	4.8		CRYSTALS WERE GROWN BY HANGING DROP VAPOUR DIFFUSION FROM 24-26% PEG 4000, 10MM SODIUM ACETATE AT PH 4.8 AND 0.01% SODIUM AZIDE. CELL PARAMETERS ARE NOT THOSE DETERMINED EXPERIMENTALLY. THEY WERE ADJUSTED ON THE BASIS OF THE ENGH & HUBER DICTIONARY AT THE END OF REFINEMENT. THE EXPERIMENTAL ESTIMATES WERE KNOWN TO HAVE POTENTIAL ERRORS DUE TO INACCURACIES IN THE CRYSTAL-TO-DETECTOR AND WAVELENGTH CALIBRATION., vapor diffusion - hanging drop