2CJT

Structural Basis for a Munc13-1 Homodimer - Munc13-1 - RIM Heterodimer Switch: C2-domains as Versatile Protein-Protein Interaction Modules

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 19-BM
Synchrotron site	APS
Beamline	19-BM
Temperature [K]	100
Detector technology	CCD
Collection date	2004-10-20
Detector	CUSTOM
Spacegroup name	P 1 21 1
Unit cell lengths	43.558, 127.144, 50.739
Unit cell angles	90.00, 90.27, 90.00

Refinement procedure

Resolution	20.000 - 1.440
R-factor	0.16
Rwork	0.160
R-free	0.18800
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.020
RMSD bond angle	1.842
Data reduction software	HKL-2000
Data scaling software	HKL-2000
Phasing software	PHASER
Refinement software	REFMAC (5.2.0003)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	47.120	1.470
High resolution limit [Å]	1.440	1.440
Rmerge	0.060	0.360
Number of reflections	99080
<I/σ(I)>	24.1	3
Completeness [%]	99.7	97.1
Redundancy	4.3	2.9

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	4.5	293	VAPOR DIFFUSION; HANGING DROP; PROTEIN: 12 MG/ML MUNC13-1 IN 30 MM TRIS, 150 MM NACL AND 1 MM TCEP, PH 7.4; RESERVOIR: 0.4 M MAGNESIUM FORMATE, 0.1 M SODIUM ACETATE (PH 4.5); DROP: 1 MICROLITER PROTEIN PLUS 1 MICROLITER RESERVOIR; TEMPERATURE: 20 DEGREES CELSIUS; CRYSTALS APPEARED OVERNIGHT AND GREW TO A FINAL SIZE OF ABOUT 0.05 MM X 0.05 MM X 0.35 MM WITHIN 3 DAYS.