The coreexcited quartet and doublet spectra of B 111, produced by foil excitation of fast B'-ion beams, have been studied in the wavelength region 300-63OOA. A large number of new transitions have been observed, for the first time allowing a detailed test ot theoretically predicted coreexcited B I11 4Land 'L-term schemes. For a number of quartet states, the line assignments are supported by lifetime measurements. All the assigned, core-excited spectral lines are in excellent agreement with theoretical predictions by Chung et al. These predictions have been extended to include quartet states with L > 2.

Crystals of bovine adenosine deaminase (ADA) grown over a two-week period in the presence of an inhibitor (ADA complex) were found to be of low quality for X-ray diffraction analysis. Furthermore, ADA incubated in the absence of an inhibitor (ADA native) did not form any crystals using conventional crystallization methods. A solution-stirring technique was used to obtain high-quality ADA complex and ADA native crystals. The crystals obtained using this technique were found to be of high quality and were shown to have high structural resolution for X-ray diffraction analyses. The results reported here indicate that the solution-stirring technique promotes nucleation and improves the quality of protein crystals.

We employ surface topographies and phase images to investigate InN nanodots. The samples are annealed at 450, 500 and 550 . The results reveal that the statistical distributions of number density and mean size depend on annealing ambient. The behaviours of thermal annealing between InN films and InN nanodots are distinguishable: the alloying process of InN and GaN not only occurs in InN platelets, but also in InN nanodots once the samples are annealed at the growth temperature of InN nanodots, while the main change in InN films is the decomposition of InN into In droplets and N 2 .

We previously developed an effective method for growing large, high-quality protein crystals. The method, which we call the floating and stirring technique (FAST), enables us to grow crystals on an insoluble and very dense liquid without contacting the growth vessel, and to stir a protein solution mildly. Our newly designed technique, Micro-FAST, makes FAST suitable for practical use. Micro-FAST enables us to reduce the sample volume and is applied to the vapor diffusion technique. Crystals grown by Micro-FAST demonstrated excellent X-ray diffraction with high resolution.

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