2V0P

The Structure of Tap42 Alpha4 Subunit

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE BM14
Synchrotron site	ESRF
Beamline	BM14
Temperature [K]	100
Detector technology	CCD
Collection date	2006-05-01
Detector	MARRESEARCH
Spacegroup name	P 1
Unit cell lengths	44.633, 48.308, 71.960
Unit cell angles	81.31, 87.94, 69.83

Refinement procedure

Resolution	71.070 - 1.800
R-factor	0.239
Rwork	0.238
R-free	0.25600
Structure solution method	SAD
RMSD bond length	0.019
RMSD bond angle	1.558
Data reduction software	MOSFLM
Data scaling software	SCALA
Phasing software	SHELX
Refinement software	REFMAC (5.2.0019)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	1.900
High resolution limit [Å]	1.800	1.800
Rmerge	0.050	0.460
Number of reflections	49867
<I/σ(I)>	15.6	2.6
Completeness [%]	96.4	96.4
Redundancy	4.4	4.4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	6.5	293	THE PROTEIN WAS CONCENTRATED TO 10 MG/ML BEFORE CRYSTALLIZATION. CRYSTALS WERE GROWN AT 20C USING THE HANGING DROP METHOD. ONE MICROLITRE OF PROTEIN WAS MIXED WITH AN EQUAL VOLUME OF CRYSTALLIZATION BUFFER: 20% (W/V) PEG 8000, 0.1 M SODIUM CACODYLATE PH 6.5, 0.2 M MAGNESIUM ACETATE AND 2MM DTT. CRYSTALS WERE OPTIMISED BY SEEDING.