Table 2. Reference subset.

Data set	Description
10.15785/SBGRID/5Boggon LaboratoryReference Case 1:MR/Multi-crystal averaging.	Data sets from 5 crystals of SNX17 FERM domain in complex with a peptide corresponding to KRIT1's NPxY2 motif. Separate integration of the data sets and scaling together allows a complete 3.0 Å data set for molecular replacement solution (original paper used 4GXB as a search model) and structure refinement.
10.15785/SBGRID/117Baxter LaboratoryReference Case 2:MR/Low resolution, twinned with rotational pseudosymmetry.	3.70 Å data set collected on a crystal of thioester-containing protein 1 *S1 allele (TEP1*S1). Initial data processing suggested P43212, but one of the two molecules (∼1300 aa. each) in the ASU overlapped with its symmetry-mate. Comparison of alternative scenarios in refinement identified the true space group as P43 with twinning and rotational pseudosymmetry. Refinement was completed with TLS, NCS (local) and external restraints derived by ProSMART65 using TEP1*R1 (PDB 4D94) as reference.
10.15785/SBGRID/62Modis LaboratoryReference case 3:U SAD/Low resolution.	4.5 Å data set of a uranyl acetate derivative used for a challenging structure determination by SAD. Certain images had streaky features and were excluded from data reprocessing. The height and definition of peaks in anomalous difference Patterson maps was improved by omitting certain images near the end of the data collection run.
10.15785/SBGRID/111 Ferré-D'Amaré LaboratoryReference Case 4:Ba/K SAD; 91 nt RNA-chromophore complex.	2.5 Å data set collected at ALS BL 5.0.2 using 6.0 keV X-rays from a crystal of 'Spinach' a fluorescent RNA analogue of GFP. Although anomalous signal was very weak, a heavy atom substructure comprised of one barium and six potassium ions resulted in good quality SAD electron density maps.
10.15785/SBGRID/3Sliz LaboratoryReference Case 5:Zn SAD; 4 Zn/ASUprotein/RNA complex.	2.9 Å Zn SAD data set was sufficient to determine a crystal structure of Lin28/let-7d protein-microRNA complex. X-ray beam size was adjusted to maximize flux and minimize radiation damage. One swapped-dimer is located in each asymmetric unit. Two native zinc atoms are located in each tandem CCHC zinc knuckles domain.
10.15785/SBGRID/123Heldwein LaboratoryReference Case 6:3.29-Å SeMet SAD9 Se/ASU	This 3.29-Å selenomethionine SAD data set, collected at 0.9789 Å wavelength at BNL X25 beamline, was sufficient to determine the phases and to trace the structure of HSV-2 gH/gL complex66. There are 9 Se sites in the ASU. During integration in HKL2000, χ2 appeared very large for some sectors of the data set. These correlated with crystal orientation and likely resulted from a large difference in cell edges (a=b=88 Å versus c=333 Å).
10.15785.SBGRID/179Schwartz LaboratoryReference Case 7:MR-SAD at 7.0 Å	Contaminating E.coli protein 4FCC_A, acting as a crystallization chaperone, was found readily by MR. Using these MR phases seven (Ta6Br12)2+-positions could be found in the 8.8 Å derivative data set 180. The combined MR-SAD phases were sufficient to position two copies of Nup37 (4FHL) and two copies of Nup120 in the asymmetric unit.
10.15785/SBGRID/21810.15785/SBGRID/78Rudenko LaboratoryReference Case 8:MR-SAD at 2.65 Å(44 Se atoms/ASU)	3.25 Å data set (#218) from a crystal of the selenomethionyl neurexin 1alpha ectodomain and 2.65 Å higher resolution native data set (#78), both collected at APS using multiple settings. The structure has 2 molecules/ASU with a total of 14 ordered domains and ∼2,000 residues. Molecular replacement successfully placed 8 LNS domains (using a single LNS domain as a search model, i.e. ∼9% of the scattering mass) generating phases which could be used to reveal 37 out of 44 Se atoms/ASU in the 3.25 Å SeMet SAD data set. Refinement was completed using data set #78.
10.15785/SBGRID/9Tao LaboratoryReference case 9:3.25 Å data set used for MR with a 9-Å cryo-EM envelope	A 3.25-Å resolution data set was collected at APS LS-CAT. The structure was determined by molecular replacement using a 9-Å resolution cryo-EM reconstruction as a phasing model. Solvent flattening and 15-fold noncrystallographic symmetry averaging were applied during phase extension.
10.15785/SBGRID/83Drennan LaboratoryReference Case 10:MR/large unit cell, anisotropic.	Diffraction data from different regions of a crystal of Isobutyryl-coenzyme A mutase fused, a 250 kDa dimeric enzyme. This crystal had a large unit cell (a,b=319 Å, c=344 Å) and the data were anisotropic. Separate integration of the 6 wedges with individually adjusted resolution limits and scaling together yields a complete 3.35 Å data set that can be used for molecular replacement.
10.15785/SBGRID/125Kruse Laboratory(data collected in Kobilka Laboratory)Reference Case 11:MR, lipidic cubic phase	Diffraction data for lipidic cubic phase crystals of human M2 muscarinic acetylcholine receptor bound to the agonist iperoxo, the allosteric modulator LY2119620, and the conformationally-selective nanobody Nb9-8.
DOI:10.15785/SBGRID/68Fraser LaboratoryReference case 12:X-ray diffuse scattering	1.2 Å data set collected at SSRL provides a high-resolution standard data set of the enzyme Cyclophilin to examine the influence of data collection temperature to compare with XFEL data, and to measure X-ray diffuse scattering.

MR, molecular replacement; SAD, Single-wavelength Anomalous Diffraction.

12 X-ray diffraction data sets from the SBDG pilot collection were identified as particularly suitable for software testing and teaching activities. In addition, data sets from molecular dynamics, lattice light-sheet microscopy and MicroED represent an invaluable subset.