• 약학회지
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• 제40권4호
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• pp.375-381
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• 1996

Five crystal modification of droperidol were prepared by recrystallization. They were characterized by UV spectrophotometer, DSC, and X-ray crystallography. Their dissolution pa tterns were also investigated. After storage of 2 months at 100% humidity, all polymorphic modifications were transformed.

• Journal of Pharmaceutical Investigation
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• 제28권2호
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• pp.115-119
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• 1998

Five polymorphic modifications of Cephradin were prepared by recrystallization from organic solvents. The isolated crystal forms were characterized by differential scanning calorimetry (DSC), thermogravimetric analysis (TGA) and X-ray crystallography powder diffractometry. Modificaition 1 was the most stable form and decomposed at $201.3^{\circ}C$. Modification 3 and 4 were metastable. The dissolution of modification 3 and 4 was faster than that of marketed form.

• Bulletin of the Korean Chemical Society
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• 제29권7호
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• pp.1369-1373
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• 2008

A stable twist boat conformation of thiane S-oxide 1a in solid state and in solution was unambiguously determined by single crystal X-ray crystallography and solution NMR analyses. On the contrary, the thiane Sdioxide 2 which was obtained from the oxidation of corresponding thiane S-oxide 1a was confirmed to adopt a regular chair conformation.

• 한국결정학회지
• /
• 제1권1호
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• pp.57-59
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• 1990

International Tables of X-Ray Crystallography Vol.IV(1974) Table 2.3.2에 오자가 있다. 점군 422의 등가반사면들은 hkl=hkl=hkl=hkl=hkl=khl=khl=khl이다.

• Journal of Pharmaceutical Investigation
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• 제30권3호
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• pp.201-205
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• 2000

Three new polymorphic modifications were prepared by recrystallization under various conditions and characterized by DSC and X-ray crystallography. In pH 4.0 buffer at $37{\pm}0.5^{\circ}C$, the polymorphic modifications showed significant differences in the dissolution rate. The dissolution rate of Mod. 4, amorphous form, was faster than that of marketed cefaclor (Mod. 1). When all modifications were stored at 52% RH, 95% RH and in silica gel desiccator, any polymorphic transformation was not observed.

• Journal of Pharmaceutical Investigation
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• 제30권4호
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• pp.289-293
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• 2000

Three polymorphic modifications and one amorphous form were prepared by recrystallization under various conditions and characterized by DSC and X-ray crystallography. At $37{\pm}0.5^{\circ}C$, the polymorphic modifications showed significant differences in the dissolution rate. The dissolution rate of Mod. 4, amorphous form, was faster than that of other polymorphic modifications. When all modifications were stored at 52% RH, 95% RH, and in silica gel desiccator, amorphous form was transformed at 95% humidity condition.

• 한국결정학회지
• /
• 제12권1호
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• pp.25-30
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• 2001

• 한국결정학회지
• /
• 제14권2호
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• pp.115-121
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• 2003

• 한국전자현미경학회:학술대회논문집
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• 한국현미경학회 2000년도 제31차 추계학술대회
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• pp.65-65
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• 2000

• Macromolecular Research
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• 제14권2호
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• pp.140-145
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• 2006

E-science refers to the large-scale science that will increasingly be carried out through distributed global collaborations enabled by the Internet. The Grid is a service-oriented architecture proposed to provide access to very large data collections, very large scale computing resources and remote facilities. Web services, which are server applications, enable online access to service providers. Web portal interfaces can further hide the complexity of accessing facility's services. The main use of synchrotron radiation (SR) facilities by protein crystallographers is to collect the best possible diffraction data for reasonably well defined problems. Significant effort is therefore being made throughout the world to automate SR protein crystallography facilities so scientists can achieve high throughput, even if they are not expert in all the techniques. By applying the above technologies, the e-HTPX project, a distributed computing infrastructure, was designed to help scientists remotely plan, initiate and monitor experiments for protein crystallographic structure determination. A description of both the hardware and control software is given together in this paper.