Development of an automated ultrasonic spray pyrolysis system and the growth of Cu2ZnSnS4 thin films

An automated ultrasonic spray pyrolysis system is fabricated for the growth of thin films. The system is equipped with x-y movement and enables film deposition in different patterns and spray rates. Cu-2(Zn,Sn)S-4 (CZTS) films are deposited using this setup. The substrate temperature (T-s) is varied from 240 to 490 degrees C. Kesterite CZTS phase is observed in all the films together with binary phases. The films prepared at T-s <340 degrees C showed SnxSy phase and those at T-s >340 degrees C showed Cu2S phase. Sulfur incorporation is maximum (40%) at 440 degrees C and the films showed better morphology. The Cu and S concentrations are varied to remove binary phases. Depth wise elemental analysis confirmed the existence of single phase CZTS. p-Type CZTS films of resistivity in the range of 10(2)-10(3) Omega cm are obtained. (C) 2015 Elsevier B.V. All rights reserved.

Rapid NMR Assignments of Proteins by Using Optimized Combinatorial Selective Unlabeling

A new approach for rapid resonance assignments in proteins based on amino acid selective unlabeling is presented. The method involves choosing a set of multiple amino acid types for selective unlabeling and identifying specific tripeptides surrounding the labeled residues from specific 2D NMR spectra in a combinatorial manner. The methodology directly yields sequence specific assignments, without requiring a contiguously stretch of amino acid residues to be linked, and is applicable to deuterated proteins. We show that a 2D N-15,H-1]HSQC spectrum with two 2D spectra can result in approximate to 50% assignments. The methodology was applied to two proteins: an intrinsically disordered protein (12kDa) and the 29kDa (268 residue) -subunit of Escherichia coli tryptophan synthase, which presents a challenging case with spectral overlaps and missing peaks. The method can augment existing approaches and will be useful for applications such as identifying active-site residues involved in ligand binding, phosphorylation, or protein-protein interactions, even prior to complete resonance assignments.