The downsizing of solder balls results in larger interfacial intermetallic compound (IMC) grains and less Cu substrate consumption in lead-free soldering on Cu substrates. This size effect on the interfacial reaction is experimentally demonstrated and theoretically analyzed using Sn-3.0Ag-0.5Cu and Sn-3.5Ag solder balls. The interfacial reaction between the Sn-xAg-yCu solders and Cu substrates is a dynamic response to a combination of effects of interfacial IMC growth, Cu substrate consumption and composition variation in the interface zone. A concentration gradient controlled (CGC) kinetics model is proposed to explain the combined effects. The concentration gradient of Cu at the interface, which is a function of solder volume, initial Cu concentration and reaction time, is the root cause of the size effect. We found that a larger Cu concentration gradient results in smaller Cu6Sn5 grains and more consumption of Cu substrate. According to our model, the growth kinetics of interfacial Cu6Sn5 obeys a t1/3 law when the molten solder has approached the solution saturation, and will be slower otherwise due to the interfering dissolution mechanism. The size effect introduced in this model is supported by a good agreement between theoretical and experimental results. Finally, the scope of application of this model is discussed.

A general and efficient method for the synthesis of quinazolinones, quinoxalinones, benzooxazinones, and benzothiazoles from the reactions of α-keto acids with 2-aminobenzamides, benzene-1,2-diamines, 2-aminophenols, and 2-aminobenzenethiols, respectively, is described. The reactions were conducted under catalyst-free conditions, using water as the sole solvent with no additive required, and successfully applied to the synthesis of sildenafil. More importantly, these reactions can be conducted on a mass scale, and the products can be easily purified through filtration and washing with ethanol (or crystallized).

The Sn-Bi base lead-free solders are proposed as one of the most popular alloys due to the low melting temperature (eutectic point: 139°C) and low cost. However, they are not widely used because of the lower wettability, fatigue resistance, and elongation compared to traditional Sn-Pb solders. So the alloying is considered as an effective way to improve the properties of Sn-Bi solders with the addition of elements (Al, Cu, Zn, Ga, Ag, In, Sb, and rare earth) and nanoparticles. In this paper, the development of Sn-Bi lead-free solders bearing elements and nanoparticles was reviewed. The variation of wettability, melting characteristic, electromigration, mechanical properties, microstructures, intermetallic compounds reaction, and creep behaviors was analyzed systematically, which can provide a reference for investigation of Sn-Bi base solders.

Received 7 June 2013; accepted 21 June 2013AbstractElectron crystallography is an important method for determining the structure of membrane proteins. In this paper, we show the impact of a carbon sandwich preparation on the preservation of crystalline sample quality, using characteristic examples of two-dimensional (2D) crystals from gastric H+,K+-ATPase and their analyzed images. Compared with the ordinary single carbon support film preparation, the carbon sandwich preparation dramatically enhanced the resolution of images from flat sheet 2D crystals. As water evaporation is restricted in the carbon-sandwiched specimen, the improvement could be due to the strong protective effect of the retained water against drastic changes in the environment surrounding the specimen, such as dehydration and increased salt concentrations. This protective effect by the carbon sandwich technique helped to maintain the inherent and therefore best crystal conditions for analysis. Together with its strong compensation effect for the image shift due to beam-induced specimen charging, the carbon sandwich technique is a powerful method for preserving crystals of membrane proteins with larger hydrophilic regions, such as H+,K+-ATPase, and thus constitutes an efficient and high-quality method for collecting data for the structural analysis of these types of membrane proteins by electron crystallography.