3TYT

Crystal structure of a Heterogeneous nuclear ribonucleoprotein L (Hnrpl) from Mus musculus at 1.60 A resolution

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SSRL BEAMLINE BL14-1
Synchrotron site	SSRL
Beamline	BL14-1
Temperature [K]	100
Detector technology	CCD
Collection date	2011-06-03
Detector	MARMOSAIC 325 mm CCD
Spacegroup name	P 64 2 2
Unit cell lengths	127.424, 127.424, 80.652
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	41.709 - 1.600
R-factor	0.1777
Rwork	0.176
R-free	0.20410
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.015
RMSD bond angle	1.623
Data reduction software	MOSFLM
Data scaling software	SCALA (3.3.15)
Phasing software	MOLREP
Refinement software	REFMAC (5.5.0110)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	41.709	41.709	1.690
High resolution limit [Å]	1.600	5.060	1.600
Rmerge		0.039	1.170
Rmeas	0.084	0.043	1.281
Rpim	0.025	0.013	0.386
Total number of observations	558136	17550	79741
Number of reflections	51213
<I/σ(I)>	15.4	45.3	2.1
Completeness [%]	100.0	98.8	100
Redundancy	10.9	9.8	10.9

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	3.6	277	2.0M NaCl, 10.0% PEG-6000, No Buffer pH 3.6, VAPOR DIFFUSION, SITTING DROP, NANODROP, temperature 277K