{"title":"Carl-Ivar Brändén (1934–2004)","authors":"Jane Smith","doi":"10.1107/S0907444904018189","DOIUrl":null,"url":null,"abstract":"Science lost a valued citizen on 28 April 2004 when Carl-Ivar BraÈndeÂn succumbed to lung cancer following an 18-month battle. BraÈndeÂn was a prominent member of the structural biology community. Carl grew up in Lapland in northern Sweden, where his father was the teacher in a one-room schoolhouse. His active and free childhood instilled a life-long love of exploration and nature. At the same time he developed a strong desire to expand his horizons beyond the frozen north, and decided that a good education was his ticket to rest of the world. This led him, from age 13 onward, to schooling away from his family and eventually to Uppsala University. Carl's higher education in science was characterized by an ability to take opportunities where and when he found them and by an intellect that was restless unless challenged with an important problem. He began studying mathematics and physics at Uppsala University, but, bored by the undergraduate physics curriculum and inspired by Linus Pauling's texts, he switched to chemistry. An early and important mentor was Professor Ingvar Lindqvist, who invited Carl into his laboratory for PhD studies in chemical crystallography. During his studies with Lindqvist, Carl co-authored a least-squares re®nement program for the ®rst Swedish electronic computer and used it to re®ne the structures of several metal coordination complexes he had solved. Again bored and on the verge of leaving both crystallography and chemistry, Carl was enticed to the new ®eld of protein crystallography by a lecture course in biochemistry. Thus, he leapt at a postdoctoral opportunity to develop re®nement methods for myoglobin with John Kendrew at the MRC laboratory in Cambridge, UK, where in 1962 joined the ®rst generation of protein crystallographers. In the company of Max Perutz, John Kendrew, Francis Crick, Fred Sanger, Michael Rossmann, David Blow, Sydney Brenner, Aaron Klug, Lubert Stryer, Richard Henderson and many others, Carl experienced the heady early days of molecular and structural biology and celebrated the Nobel prizes to Crick, Watson and Wilkins, and to Perutz and Kendrew.","PeriodicalId":6895,"journal":{"name":"Acta Crystallographica Section D: Biological Crystallography","volume":null,"pages":null},"PeriodicalIF":2.2000,"publicationDate":"2004-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Acta Crystallographica Section D: Biological Crystallography","FirstCategoryId":"99","ListUrlMain":"https://doi.org/10.1107/S0907444904018189","RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Science lost a valued citizen on 28 April 2004 when Carl-Ivar BraÈndeÂn succumbed to lung cancer following an 18-month battle. BraÈndeÂn was a prominent member of the structural biology community. Carl grew up in Lapland in northern Sweden, where his father was the teacher in a one-room schoolhouse. His active and free childhood instilled a life-long love of exploration and nature. At the same time he developed a strong desire to expand his horizons beyond the frozen north, and decided that a good education was his ticket to rest of the world. This led him, from age 13 onward, to schooling away from his family and eventually to Uppsala University. Carl's higher education in science was characterized by an ability to take opportunities where and when he found them and by an intellect that was restless unless challenged with an important problem. He began studying mathematics and physics at Uppsala University, but, bored by the undergraduate physics curriculum and inspired by Linus Pauling's texts, he switched to chemistry. An early and important mentor was Professor Ingvar Lindqvist, who invited Carl into his laboratory for PhD studies in chemical crystallography. During his studies with Lindqvist, Carl co-authored a least-squares re®nement program for the ®rst Swedish electronic computer and used it to re®ne the structures of several metal coordination complexes he had solved. Again bored and on the verge of leaving both crystallography and chemistry, Carl was enticed to the new ®eld of protein crystallography by a lecture course in biochemistry. Thus, he leapt at a postdoctoral opportunity to develop re®nement methods for myoglobin with John Kendrew at the MRC laboratory in Cambridge, UK, where in 1962 joined the ®rst generation of protein crystallographers. In the company of Max Perutz, John Kendrew, Francis Crick, Fred Sanger, Michael Rossmann, David Blow, Sydney Brenner, Aaron Klug, Lubert Stryer, Richard Henderson and many others, Carl experienced the heady early days of molecular and structural biology and celebrated the Nobel prizes to Crick, Watson and Wilkins, and to Perutz and Kendrew.
期刊介绍:
Acta Crystallographica Section D welcomes the submission of articles covering any aspect of structural biology, with a particular emphasis on the structures of biological macromolecules or the methods used to determine them.
Reports on new structures of biological importance may address the smallest macromolecules to the largest complex molecular machines. These structures may have been determined using any structural biology technique including crystallography, NMR, cryoEM and/or other techniques. The key criterion is that such articles must present significant new insights into biological, chemical or medical sciences. The inclusion of complementary data that support the conclusions drawn from the structural studies (such as binding studies, mass spectrometry, enzyme assays, or analysis of mutants or other modified forms of biological macromolecule) is encouraged.
Methods articles may include new approaches to any aspect of biological structure determination or structure analysis but will only be accepted where they focus on new methods that are demonstrated to be of general applicability and importance to structural biology. Articles describing particularly difficult problems in structural biology are also welcomed, if the analysis would provide useful insights to others facing similar problems.