Supporting information. Contents

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1 Qi Jiang, Chunhua Hu and Michael D. Ward* Contribution from the Molecular Design Institute, Department of Chemistry, New York University, 100 Washington Square East, New York, NY Supporting information Contents Materials and Methods X-ray Diffraction Methods and Nanocrystal Orientation Analysis Scheme S1. Schematic of the geometry for X-ray diffraction circles in the laboratory coordinates X L Y L Z L, illustrating the azimuthal angle (δ) and rotation axes (ω, ψ, ). NOTE: The Bruker GADDS software actually reports the azimuthal angle as the variable γ, with γ = 0 coinciding with the Z L direction. Therefore γ = δ o. Scheme S2. The sample translation axes XYZ and the sample coordinates h 1 h 2 h 3 with diffraction vector H hkl. Figure. S1. Image of Bruker D8 Discover GADDS X-ray microdiffractometer (μ-xrd) equipped with VÅNTEC D detector and a 0.5 mm MONOCAP beam collimator for characterization of glycine growth in AAO. Figure. S2. Configuration of reflection mode for μ-xrd equipped with a 2D detector. The interplanar angle (Φ) can be calculated with incident X-ray angle (θ 1 ), Bragg reflection angle (θ) and azimuthal angle (δ) on 2D detector. Figure. S3. Higher Bragg angle 2D μ-xrd patterns for azimuthal angle (δ) determining with α-glycine in 200 nm AAO, which has phase transition after 90% RH treatment. θ 1 = 8º, θ 2 = 35º. Table S1. Measured parameters for orientation analysis of β-glycine nanocrystals embdded in 20 nm, 100 nm and 200 nm AAO. Table S2. Measured parameters for orientation analysis of α-glycine nanocrystals embedded in 20 nm, 100 nm and 200 nm AAO with corresponding β-glycine phase transition after 90% RH treatment for 24 h. Figure. S4. 2D μ-xrd patterns with time-dependent measurement for glycine polymorphic transition in 200 nm AAO of highly oriented crystal from β to α. Figure. S5. (A) 1D PXRD patterns for time-dependent measurement for 90% RH treatment of glycine growth in 200 nm AAO. (B) Weight percentage (wt-%) for both β and α-glycine compositions during the 90% RH treatment. The software TOPAS 4.2 (Bruker AXS, 2009) with the empirical approach was S1

2 employed for Rietveld refinements to determine the phase composition. The structural models of α and β phases were obtained from the Cambridge Structure Database, i.e. REFCODE_GLYCIN04 (α, Acta Cryst. 2002, E58, o634) and REFCODE_GLYCIN35 (β, J. Chem. Phys. 1977, 59, 3901). The standard SRM 660b for powder diffraction, i.e. lanthanum hexaboride (LaB 6 ), which was certified by the National Institute of Standards and Technology (NIST), was used to calculate the empirical instrument function. The resulted instrument function parameters were later fixed for the refinement of other patterns. The whole pattern ranging from 10 to 35 were refined. Refined parameters included background as Chebyshev polynomial of fifth order and 1/x function, zero error, sample displacement, scale factor, and lattice parameters. The contribution of the AAO membrane was also refined as an amorphous phase. Figure. S6. 2D μ-xrd patterns of Time dependent measurement with β-glycine recrystallization in 200 nm AAO with addition of 5 μl water droplet on AAO membrane surface. (A) original condition with β- glycine patterns; (B) after 5 min and (C) 10 min with addition of water have no diffraction; (D) after 15 min, (E) 20 min, (F) 30 min, (G) 40 min, (H) 60 min, (I) 90 min, (J) 120 min and (K) 180 min. All of them have β-glycine diffraction patterns. (L) Intensity of (020) peak of β-glycine during the recrystallization of β-glycine in AAO. Figure. S7. 2D μ-xrd patterns for glycine growth with racemic auxiliary DL-Trp (0.3%, w/w water) in (A) 20 nm, (B) 100 nm and (C) 200 nm AAO before (left) and after (after) 90% RH treatment for 24 h. ( ) denotes for β-glycine. Table S3. Polymorph and orientations of glycine crystals embedded in AAO before and after polymorphic transition Figure. S8. Molecular structures of α-amino acids as auxiliaries. The auxiliaries abbreviation are Phe (phenylalanine), Trp (tryptophan), Met (methionine), Glu (glutamic acid), Ala (alanine), Val (valine), Leu (leucine), His (histidine), Ser (serine), Pro (proline). Table S4. Water solubility of glycine and other α-amino acids as auxiliaries at room temperature (20 C and 30 C). S2

3 Materials and Methods. Circular anodic aluminum oxide (AAO) membranes having average pore diameters of 20 nm, 100 nm and 200 nm were purchased from Whatman Inc. (Piscataway, NJ). The AAO membranes were 13 cm in diameter and 60 µm thick. Glycine was purchased from Sigma-Aldrich and used as obtained. The AAO membranes were immersed in 18% glycine solution for two hours, during which the glycine solution diffused into the pores of the membrane. After removal from solution, the outer surfaces of the membranes were carefully swabbed with a soft tissue to remove any external glycine solution residue. The membranes were then allowed to dry under ambient conditions or were dried under vacuum at approximately 0.1 mm Hg for 4 hours. The drying method did not affect the crystallization outcome. The effect of humidity on phase transitions were performed in a glove box designed for humidity regulation. X-Ray Diffraction Methods and Nanocrystal Orientation Analysis. 1 X-ray microdiffraction (μ-xrd) was performed with a Bruker D8 Discover microdiffractometer with the General Area Detector Diffraction System (GADDS) equipped with a VÅNTEC D detector and Cu-Kα source (λ = Å). The X-ray beam was monochromated with a graphite crystal and collimated with a 0.5 mm capillary collimator (MONOCAP). The AAO membrane was mounted in a horizontal configuration on a sample stage affixed to a five-circle Eulerian cradle. The alignment of the AAO membrane with the X-ray beam and detector was determined with a laser-video alignment accessory supplied by Bruker. Onedimensional diffraction patterns were generated by integrating the 2D XRD data over the entire range of azimuthal angles at each 2θ value using XRD2EVAL, a software program provided by Bruker (version ; Bruker AXS Inc., Madison, WI, 2009). Crystal structures were retrieved from the Cambridge Structural Database (Cambridge Crystallographic Data Center (CCDC), Cambridge, United Kingdom) and visualized using Mercury (also from CCDC). Mercury also was used to calculate interplanar angles in the crystal structures and to generate simulated 1D powder XRD patterns. 2D X-ray diffraction on the Bruker diffractometer encompasses three geometry spaces: diffraction space, detector space, and sample space, all which are interrelated and depicted in Scheme S1. The laboratory coordinate system, defined by X L, Y L, and Z L, is the reference for all three spaces. The direct X-ray beam propagates along X L, Z L and Y L. The azimuthal angle δ in detector space represents the location of the diffracted beam on diffraction circle. δ is calculated by a counter-clockwise rotation (left-hand rotation) when viewed along the direction X L relative to an origin at the Y L position. The coordinate (2θ, δ) on the 2D detector corresponds to the Bragg angle and orientation of the diffracting plane. The sample orientation is defined by the rotation angles ω, ψ, and ϕ. The sample translation coordinates XYZ are defined such that when ω = ψ = ϕ = 0, X = -X L, Y = Z L, and Z = Y L. Measurements described here were performed with θ 1 (incident X-ray beam angle) = θ 2 (detector angle) = 8. The sample-to-detector distance S3

4 was 150 mm. In the range 0 < 2θ 19, data could be collected across the azimuthal angle range -90 δ 90. In the range 19 < 2θ 35 data from only a portion of the half circle could be collected, with the azimuthal range decreasing with increasing 2θ. Scheme S1. Schematic of the geometry for X-ray diffraction circles in the laboratory coordinates X L Y L Z L, illustrating the azimuthal angle (δ) and rotation axes (ω, ψ, ϕ). NOTE: The Bruker GADDS software actually reports the azimuthal angle as the variable, with = 0 coinciding with the Z L direction. Therefore = δ o. Scheme S2 indicates the diffraction vector H hkl, which refers to a specific Miller plane (hkl) in the sample translation coordinates, XYZ. The direction of H hkl is determined by the orientation of the crystal plane (hkl). To simplify calculations, all vectors were converted to unit vectors. The diffraction vector H hkl (h 1, h 2, h 3 ) is defined as the following column vector: H hkl h1 h2 h 3 In the sample coordinate system, h 1, h 2 and h 3 can be expressed in terms of the Bragg angle, θ, azimuthal angle, δ, and rotation angles about the three axes, ω, ψ, and ϕ: h sin (sin sin sin cos cos ) cos sin sin cos cos cos (sin sin cos cos sin ) h 1 2 sin (cos sin sin sin cos ) cos sin cos cos cos cos (cos sin cos sin sin ) h 3 sin cos sin cos cos cos cos cos sin sin In our experimental setup, θ 1 = ω, where θ 1 is the incident angle of the x-ray beam, and ϕ = ψ = 0. The diffraction vector can thus be simplified as the following column vector: S4

5 h1 sin cos1 cos sin1cos h2 cos sin h3 sin sin1 cos cos1cos Scheme S2. The sample translation axes XYZ and the sample coordinates h 1 h 2 h 3 with diffraction vector H hkl To determine the orientations of glycine crystals within AAO pores, we examined the intensities of reflections along the azimuthal angle, δ, in the 2D diffraction patterns. For all experiments, samples were oriented such that the pore direction was parallel to the Z-axis in sample translation coordinates. In this configuration, reflections of crystal planes oriented perpendicular to the pore direction, and thus parallel to the horizontal plane, display strongest intensities at δ = 0. By identifying the crystallographic plane perpendicular to the pore direction of AAO membranes, we can determine the orientation of glycine crystals within the pores. We can further verify the self-consistency of the 2D diffraction patterns with respect to the single crystal structure of glycine by comparing the expected interplanar angles, Φ, to the difference in δ values between reflections in the observed diffraction pattern. The interplanar angle can be calculated as follows: cos a b a b where ab is the dot product of two diffraction vectors, and a b is the product of the lengths of the two vectors. For unit vectors, a b =1, allowing us to simplify the expression for the interplanar angle to cos a b In the Cartesian coordinate system, the dot product of two vectors can be defined as follows: S5

6 A ( u, v, w), B ( x, y, z) A B ux vy wz The unit vectors along X, Y, and Z are (1, 0, 0), (0, 1, 0), and (0, 0, 1), respectively, with the (0, 0, 1) vector is the perpendicular to the horizontal plane of the sample. The interplanar angle thus is can be calculated as below follows: sin cos1 cos sin1cos 0 cos cos sin 0 sin sin1 cos cos1cos sin sin1 cos cos1cos 1 For diffraction patterns collected in transmission mode (i.e. θ 1 = 0), the formula simplifies to cos cos cos which is equivalent to the previously derived definition of the interplanar angle that does not take into account the incident angle of the x-ray beam. 2 Figure S1. Image of Bruker D8 Discover GADDS X-ray microdiffractometer (μ-xrd) equipped with VÅNTEC D detector and a 0.5 mm MONOCAP beam collimator for characterization of glycine growth in AAO. S6

7 Figure S2. Configuration of reflection mode for μ-xrd equipped with a 2D detector. The interplanar angle (Φ) can be calculated with incident X-ray angle (θ 1 ), Bragg reflection angle (θ) and azimuthal angle (δ) on 2D detector. Figure S3. Higher Bragg angle 2D μ-xrd patterns for azimuthal angle (δ) determining with α-glycine in 200 nm AAO, which has phase transition after 90% RH treatment. θ 1 = 8º, θ 2 = 35º. Table S1. Measured parameters for orientation analysis of β-glycine nanocrystals embdded in 20 nm, 100 nm and 200 nm AAO. Reflection (hkl) Incident X-Ray Angle θ 1 (º) Bragg Angle 2θ (º) Azimuthal Angle δ (º) Interplanar Angle (º) β-glycine in 20, 100 and 200 nm AAO (020) perpendicular to pores (001) , (011) , (110) , (020) (021) , (120) , S7

8 Table S2. Measured parameters for orientation analysis of α-glycine nanocrystals embedded in 20 nm, 100 nm and 200 nm AAO with corresponding β-glycine phase transition after 90% RH treatment for 24 h. Reflection (hkl) Incident X-ray Angle θ 1 (º) Bragg Angle 2θ (º) Azimuthal Angle δ (º) Orientation (º) α-glycine in 20, 100 and 200 nm AAO after 90% RH ( 20 1 ) perpendicular to pores (020) , (110) , (120) , ( 21 1 ) ,-7 19 (200) , (210) , (220) , Figure S4. 2D μ-xrd patterns with time-dependent measurement for glycine polymorphic transition in 200 nm AAO of highly oriented crystal from β to α. S8

9 Figure S5. (A) 1D PXRD patterns for time-dependent measurement for 90% RH treatment of glycine growth in 200 nm AAO. (B) Weight percentage (wt-%) for both β and α-glycine compositions during the 90% RH treatment. The software TOPAS 4.2 (Bruker AXS, 2009) with the empirical approach was employed for Rietveld refinements to determine the phase composition. The structural models of α and β phases were obtained from the Cambridge Structure Database, i.e. REFCODE_GLYCIN04 (α, Acta Cryst. 2002, E58, o634) and REFCODE_GLYCIN35 (β, J. Chem. Phys. 1977, 59, 3901). The standard SRM 660b for powder diffraction, i.e. lanthanum hexaboride (LaB 6 ), which was certified by the National Institute of Standards and Technology (NIST), was used to calculate the empirical instrument function. The resulted instrument function parameters were later fixed for the refinement of other patterns. The whole pattern ranging from 10 to 35 were refined. Refined parameters included background as Chebyshev polynomial of fifth order and 1/x function, zero error, sample displacement, scale factor, and lattice parameters. The contribution of the AAO membrane was also refined as an amorphous phase. Figure S6. 2D μ-xrd patterns of Time dependent measurement with β-glycine recrystallization in 200 nm AAO with addition of 5 μl water droplet on AAO membrane surface. (A) original condition with β-glycine patterns; (B) after 5 min and (C) 10 min with addition of water have no diffraction; (D) after 15 min, (E) 20 min, (F) 30 min, (G) 40 min, (H) 60 min, (I) 90 min, (J) 120 min and (K) 180 min. All of them have β-glycine diffraction patterns. (L) Intensity of (020) peak of β-glycine during the recrystallization of β-glycine in AAO. S9

10 Figure S7. 2D μ-xrd patterns for glycine growth with racemic auxiliary DL-Trp (0.3%, w/w water) in (A) 20 nm, (B) 100 nm and (C) 200 nm AAO before (left) and after (after) 90% RH treatment for 24 h. ( ) denotes for β-glycine. S10

11 Table S3. Polymorph and orientations of glycine crystals embedded in AAO before and after polymorphic transition auxiliary a (% w/w Glycine polymorph and direction parallel to pore direction b water) Initial crystallization After 90% RH for 24 h 20nm AAO 100nm AAO 200nm AAO 20nm AAO 100nm AAO 200nm AAO None - β [010] β [010] β [010] [100] [100] [100] DL-Phe 1.2 β [001] β [001] β [001] β [001] β [001] β [001] DL-Trp 0.3 β [010] β [010] β [010] β [010] β [010] β [010] DL-Met 1.2 β [010] β [010] β [010] β [010] β [010] β [010] DL-Glu 1.2 β, random β, random β, random β, random β, random β, random DL-Ala 1.2 β [010] β [010] β [010] α [100] α [100] α [100] DL-Val 1.2 β [010] β [010] β [010] α [100] α [100] α [100] DL-Leu 0.3 β [010] β [010] β [010] α [010] β[010]+α[100] β[010]+α[100] DL-His 1.2 β [001] β [001] β [001] α [100] β[001]+α[100] β[001]+α[100] DL-Ser 1.2 β [010] β [010] β [010] α [010] β[001]+α[100] β[001]+α[100] DL-Pro 1.2 β [010] β [010] β [010] α [010] α [100] α [100] L-Phe 1.2 β[010]+α[010] β[010]+α[010] β[010]+α[010] α [010] α[010]+α[100] α[010]+α[100] L-Trp 0.3 β [010] β [010] β [010] α [100] α [100] α [100] L-Met 1.2 β[010]+α[010] β[010]+α[010] β[010]+α[010] α [010] α[010]+α[100] α[010]+α[100] L-Glu 1.2 β [010] β [001] β [001] α [100] α [100] α [100] L-Ala 1.2 β [010] β [010] β [010] α [100] α [100] α [100] L-Val 1.2 β [010] β [010] β [010] α [100] α [100] α [100] L-Leu 0.3 β[010]+α[010] β[010]+α[010] β[010]+α[010] α [010] α[010]+α[100] α[010]+α[100] L-His 1.2 β[001] β[001] β[001] α, random α [100] α [100] L-Ser 1.2 β [010] β[001] β[001] α [100] α [100] α [100] L-Pro 1.2 β[010]+α[010] β[001]+α[010] β[001]+α[010] α [010] α [100] α [100] a The auxiliaries abbreviation are Phe (phenylalanine), Trp (tryptophan), Met (methionine), Glu (glutamic acid), Ala (alanine), Val (valine), Leu (leucine), His (histidine), Ser (serine), Pro (proline). b The glycine orientation is determined by 2D μ-xrd data. Some samples have two polymorphs or two different orientations and some samples exhibit random orientations. Figure S8. Molecular structures of α-amino acids as auxiliaries. The auxiliaries abbreviation are Phe (phenylalanine), Trp (tryptophan), Met (methionine), Glu (glutamic acid), Ala (alanine), Val (valine), Leu (leucine), His (histidine), Ser (serine), Pro (proline). S11

12 Table S4. Water solubility of glycine and other α-amino acids as auxiliaries at room temperature (20 C and 30 C) 3 Water Solubilities (g/kg) Name 20 C 30 C Glycine Phenylalanine Tryptophan Methionine Glutamic acid Alanine Valine Leucine Histidine (25 C) - Serine Proline REFERENCES (1) He, B. B. Two Dimensional X-Ray Diffraction; Wiley Inc: New York, (2) Cullity, B. D. Elements of X-Ray Diffraction; Addison-Wesley: Reading, MA, (3) Lundblad, R. L., Macdonald, F. M. (eds.) Handbook of Biochemistry and Molecular Biology (Fourth Edition); CRC Press: Boca Raton, FL, (4) S12