6VS4

Crystal structure of ADP RIBOSYLATION FACTOR-LIKE GTP BINDING PROTEIN /Small COPII coat GTPase SAR1 from Encephalitozoon cuniculi in complex with GDP

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	CLSI BEAMLINE 08ID-1
Synchrotron site	CLSI
Beamline	08ID-1
Temperature [K]	100
Detector technology	CCD
Collection date	2011-09-20
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	0.9795
Spacegroup name	P 43 21 2
Unit cell lengths	65.190, 65.190, 307.710
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	45.590 - 2.400
R-factor	0.1843
Rwork	0.180
R-free	0.23500
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	MR rosetta based on top 16 HHPRED results
RMSD bond length	0.004
RMSD bond angle	0.677
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	MR-Rosetta
Refinement software	PHENIX (1.17.1)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000	50.000	2.460
High resolution limit [Å]	2.400	10.730	2.400
Rmerge	0.053	0.024	0.558
Rmeas	0.057	0.027	0.600
Number of reflections	27225	381	1952
<I/σ(I)>	21.49	48.63	3.29
Completeness [%]	99.7	92	99.9
Redundancy	7.025	5.231	7.352
CC(1/2)	0.999	0.999	0.933

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	6.5	290	RigakuReagents JCSG+ screen, condition B10 + 10% RigakuReagents ADDIT G7: 50% (V/V) PEG 200, 200mM MgCl2, 100mM Na-cacodylate pH 6.5 + 10mM spermine: EncuA.00324.a.MB1.PW30297 at 12mg/ml + 5mM GDP: cryo: 20% EG: tray: 225442g7: puck txl1-11.