6AOL

Structure of molecular chaperone Grp94 bound to selective inhibitor methyl 3-chloro-2-(2-{2-[(4-fluorophenyl)methyl]phenyl}ethyl)-4,6-dihydroxybenzoate

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 22-BM
Synchrotron site	APS
Beamline	22-BM
Temperature [K]	197.5
Detector technology	CCD
Collection date	2017-06-07
Detector	MARMOSAIC 225 mm CCD
Wavelength(s)	1.00000
Spacegroup name	P 21 21 2
Unit cell lengths	65.599, 96.897, 42.953
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	39.268 - 2.764
R-factor	0.211
Rwork	0.207
R-free	0.27930
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2gfd
RMSD bond length	0.009
RMSD bond angle	1.097
Data reduction software	XDS
Data scaling software	SCALA
Phasing software	PHASER
Refinement software	PHENIX ((1.10.1_2155: ???))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	39.270	2.863
High resolution limit [Å]	2.760	2.760
Rmerge	0.022	0.206
Number of reflections	7358
<I/σ(I)>	19.3
Completeness [%]	98.0
Redundancy	2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.8	289	30 mg/mL protein in 100 mM bicine, pH 7.8 mixed 1:1 with mother liquor (35-39% PEG400, 7.5-10% glycerol, 100 mM bicine, pH 7.8, 75 mM magnesium chloride, crystals harvested into mother liquor + 2 mM inhibitor, soaked for 4 days. Afterward, glycerol was added to 25% and crystals were harvested and immediately cryocooled with liquid nitrogen.