6AOM

Structure of molecular chaperone Grp94 bound to selective inhibitor methyl 2-[2-(2-benzylphenyl)ethyl]-3-chloro-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 21
Unit cell lengths	65.454, 84.233, 94.966
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	35.420 - 2.870
R-factor	0.2075
Rwork	0.200
R-free	0.27160
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2gfd
RMSD bond length	0.010
RMSD bond angle	1.235
Data reduction software	HKL-3000
Data scaling software	HKL-3000
Phasing software	PHASER
Refinement software	PHENIX ((1.10.1_2155: ???))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	35.420	2.972
High resolution limit [Å]	2.870	2.870
Rmerge	0.142	0.404
Number of reflections	12437
<I/σ(I)>	26.9
Completeness [%]	99.0
Redundancy	13.3

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.