4R0Y

Structure of Maltose-binding Protein Fusion with the C-terminal GH1 domain of Guanylate Kinase-associated Protein from Rattus norvegicus

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	PAL/PLS BEAMLINE 7A (6B, 6C1)
Synchrotron site	PAL/PLS
Beamline	7A (6B, 6C1)
Temperature [K]	100
Detector technology	CCD
Collection date	2013-11-02
Detector	ADSC QUANTUM 270
Wavelength(s)	0.97857
Spacegroup name	P 21 21 2
Unit cell lengths	99.110, 158.676, 65.494
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	39.520 - 2.000
R-factor	0.243
Rwork	0.243
R-free	0.28100
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1omp
RMSD bond length	0.006
RMSD bond angle	1.200
Data reduction software	HKL-2000
Data scaling software	HKL-2000
Phasing software	MOLREP
Refinement software	CNS (1.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	2.030
High resolution limit [Å]	2.000	2.000
Rmerge	0.076	0.409
Number of reflections	68103
<I/σ(I)>	45.6	3.92
Completeness [%]	97.1	80.5
Redundancy	6.9	3.9

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	5	298	0.1M Sodium Citrate pH 5.0, 15% PEG 1500, 0.1M NaCl, VAPOR DIFFUSION, HANGING DROP, temperature 298K