2FMU

Crystal structure of a tat-interacting protein homologue (htatip2, aw111545, cc3, tip30) from mus musculus at 2.30 A resolution

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ALS BEAMLINE 8.3.1
Synchrotron site	ALS
Beamline	8.3.1
Temperature [K]	100
Detector technology	CCD
Collection date	2005-10-11
Detector	ADSC QUANTUM 210
Wavelength(s)	1.01995
Spacegroup name	P 41 21 2
Unit cell lengths	56.628, 56.628, 160.860
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	27.970 - 2.300
R-factor	0.206
Rwork	0.203
R-free	0.26500
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2bka
RMSD bond length	0.016
RMSD bond angle	1.427
Data reduction software	MOSFLM
Data scaling software	SCALA
Phasing software	MOLREP (V. 1)
Refinement software	REFMAC (5.2.0005)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	27.970	27.970	2.360
High resolution limit [Å]	2.300	10.290	2.300
Rmerge	0.072	0.019	0.712
Number of reflections	12397
<I/σ(I)>	9.4	29.9	1.1
Completeness [%]	99.9		100
Redundancy	6.4	4.6	5.8

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP, NANODROP	9.5	277	20.0% PEG-8000, 0.01M spermine tetra-HCl, 0.1M CHES, pH 9.5, VAPOR DIFFUSION, SITTING DROP, NANODROP, temperature 277K